Frechin Mathieu, Enkler Ludovic, Tetaud Emmanuel, Laporte Daphné, Senger Bruno, Blancard Corinne, Hammann Philippe, Bader Gaétan, Clauder-Münster Sandra, Steinmetz Lars M, Martin Robert Pierre, di Rago Jean-Paul, Becker Hubert Dominique
Expression of nuclear and mitochondrial genes encoding ATP synthase is synchronized by disassembly of a multisynthetase complex. Journal Article
In: Molecular cell, vol. 56, no. 6, pp. 763–776, 2014, ISSN: 1097-4164 1097-2765, (Place: United States).
Abstract | Links | BibTeX | Tags: Cell Nucleus/genetics, Fungal, Gene Expression, Gene Expression Regulation, Mitochondria/genetics, Multienzyme Complexes, PPSE, Protein Multimerization, Proton-Translocating ATPases/*genetics/metabolism, RNA-Binding Proteins/physiology, Saccharomyces cerevisiae Proteins/physiology, Saccharomyces cerevisiae/enzymology/*genetics
@article{frechin_expression_2014,
title = {Expression of nuclear and mitochondrial genes encoding ATP synthase is synchronized by disassembly of a multisynthetase complex.},
author = {Mathieu Frechin and Ludovic Enkler and Emmanuel Tetaud and Daphné Laporte and Bruno Senger and Corinne Blancard and Philippe Hammann and Gaétan Bader and Sandra Clauder-Münster and Lars M Steinmetz and Robert Pierre Martin and Jean-Paul di Rago and Hubert Dominique Becker},
doi = {10.1016/j.molcel.2014.10.015},
issn = {1097-4164 1097-2765},
year = {2014},
date = {2014-12-01},
journal = {Molecular cell},
volume = {56},
number = {6},
pages = {763--776},
abstract = {In eukaryotic cells, oxidative phosphorylation involves multisubunit complexes of mixed genetic origin. Assembling these complexes requires an organelle-independent synchronizing system for the proper expression of nuclear and mitochondrial genes. Here we show that proper expression of the F1FO ATP synthase (complex V) depends on a cytosolic complex (AME) made of two aminoacyl-tRNA synthetases (cERS and cMRS) attached to an anchor protein, Arc1p. When yeast cells adapt to respiration the Snf1/4 glucose-sensing pathway inhibits ARC1 expression triggering simultaneous release of cERS and cMRS. Free cMRS and cERS relocate to the nucleus and mitochondria, respectively, to synchronize nuclear transcription and mitochondrial translation of ATP synthase genes. Strains releasing asynchronously the two aminoacyl-tRNA synthetases display aberrant expression of nuclear and mitochondrial genes encoding subunits of complex V resulting in severe defects of the oxidative phosphorylation mechanism. This work shows that the AME complex coordinates expression of enzymes that require intergenomic control.},
note = {Place: United States},
keywords = {Cell Nucleus/genetics, Fungal, Gene Expression, Gene Expression Regulation, Mitochondria/genetics, Multienzyme Complexes, PPSE, Protein Multimerization, Proton-Translocating ATPases/*genetics/metabolism, RNA-Binding Proteins/physiology, Saccharomyces cerevisiae Proteins/physiology, Saccharomyces cerevisiae/enzymology/*genetics},
pubstate = {published},
tppubtype = {article}
}
Schwarzmüller Tobias, Ma Biao, Hiller Ekkehard, Istel Fabian, Tscherner Michael, Brunke Sascha, Ames Lauren, Firon Arnaud, Green Brian, Cabral Vitor, Marcet-Houben Marina, Jacobsen Ilse D, Quintin Jessica, Seider Katja, Frohner Ingrid, Glaser Walter, Jungwirth Helmut, Bachellier-Bassi Sophie, Chauvel Murielle, Zeidler Ute, Ferrandon Dominique, Gabaldón Toni, Hube Bernhard, d'Enfert Christophe, Rupp Steffen, Cormack Brendan, Haynes Ken, Kuchler Karl
Systematic phenotyping of a large-scale Candida glabrata deletion collection reveals novel antifungal tolerance genes Journal Article
In: PLoS Pathog., vol. 10, no. 6, pp. e1004211, 2014, ISSN: 1553-7374.
Abstract | Links | BibTeX | Tags: Antifungal Agents, Azoles, Biofilms, Candida glabrata, Candidiasis, Cell Wall, Drug Resistance, Echinocandins, ferrandon, Fungal, Fungal Proteins, Gene Deletion, Gene Knockout Techniques, Gene Library, M3i, Microbial Sensitivity Tests, Osmotic Pressure, Phenotype
@article{schwarzmuller_systematic_2014b,
title = {Systematic phenotyping of a large-scale Candida glabrata deletion collection reveals novel antifungal tolerance genes},
author = {Tobias Schwarzmüller and Biao Ma and Ekkehard Hiller and Fabian Istel and Michael Tscherner and Sascha Brunke and Lauren Ames and Arnaud Firon and Brian Green and Vitor Cabral and Marina Marcet-Houben and Ilse D Jacobsen and Jessica Quintin and Katja Seider and Ingrid Frohner and Walter Glaser and Helmut Jungwirth and Sophie Bachellier-Bassi and Murielle Chauvel and Ute Zeidler and Dominique Ferrandon and Toni Gabaldón and Bernhard Hube and Christophe d'Enfert and Steffen Rupp and Brendan Cormack and Ken Haynes and Karl Kuchler},
doi = {10.1371/journal.ppat.1004211},
issn = {1553-7374},
year = {2014},
date = {2014-01-01},
journal = {PLoS Pathog.},
volume = {10},
number = {6},
pages = {e1004211},
abstract = {The opportunistic fungal pathogen Candida glabrata is a frequent cause of candidiasis, causing infections ranging from superficial to life-threatening disseminated disease. The inherent tolerance of C. glabrata to azole drugs makes this pathogen a serious clinical threat. To identify novel genes implicated in antifungal drug tolerance, we have constructed a large-scale C. glabrata deletion library consisting of 619 unique, individually bar-coded mutant strains, each lacking one specific gene, all together representing almost 12% of the genome. Functional analysis of this library in a series of phenotypic and fitness assays identified numerous genes required for growth of C. glabrata under normal or specific stress conditions, as well as a number of novel genes involved in tolerance to clinically important antifungal drugs such as azoles and echinocandins. We identified 38 deletion strains displaying strongly increased susceptibility to caspofungin, 28 of which encoding proteins that have not previously been linked to echinocandin tolerance. Our results demonstrate the potential of the C. glabrata mutant collection as a valuable resource in functional genomics studies of this important fungal pathogen of humans, and to facilitate the identification of putative novel antifungal drug target and virulence genes.},
keywords = {Antifungal Agents, Azoles, Biofilms, Candida glabrata, Candidiasis, Cell Wall, Drug Resistance, Echinocandins, ferrandon, Fungal, Fungal Proteins, Gene Deletion, Gene Knockout Techniques, Gene Library, M3i, Microbial Sensitivity Tests, Osmotic Pressure, Phenotype},
pubstate = {published},
tppubtype = {article}
}
Niehus Sebastian, Giammarinaro Philippe, Liégeois Samuel, Quintin Jessica, Ferrandon Dominique
In: Fly (Austin), vol. 6, no. 3, pp. 193–204, 2012, ISSN: 1933-6942.
Abstract | Links | BibTeX | Tags: Animals, Apansporoblastina, Apansporoblastina/*genetics/physiology, Base Sequence, cure, Disinfection, Disinfection/methods, DNA, DNA Primers, Drosophila melanogaster/*microbiology, ferrandon, fumagillin, Fungal, Fungal/chemistry, M3i, microsporidia, obligate intracellular parasitism, PCR detection, Phylogeny, Polymerase Chain Reaction, Polymerase Chain Reaction/methods, prophylaxis, Ribosomal, Ribosomal/chemistry, Sequence Alignment, Tubulinosema ratisbonensis
@article{niehus_fly_2012b,
title = {Fly culture collapse disorder: detection, prophylaxis and eradication of the microsporidian parasite Tubulinosema ratisbonensis infecting Drosophila melanogaster},
author = {Sebastian Niehus and Philippe Giammarinaro and Samuel Liégeois and Jessica Quintin and Dominique Ferrandon},
doi = {10.4161/fly.20896},
issn = {1933-6942},
year = {2012},
date = {2012-01-01},
journal = {Fly (Austin)},
volume = {6},
number = {3},
pages = {193--204},
abstract = {Drosophila melanogaster is a robust model to investigate many biological problems. It is however prone to some infections, which may endanger fly stocks if left unchecked for. One such infection is caused by an obligate fungal intracellular parasite, Tubulinosema ratisbonensis, which can be found in laboratory stocks. Here, we identify and briefly characterize a T. ratisbonensis strain that was infesting our Drosophila cultures and that required intensive measures to contain and eradicate the infection. We describe the phenotypes of infested stocks. We also report PCR-based techniques that allow the detection of infested stocks with a high sensitivity. We have developed a high-throughput qPCR assay that allows the efficient parallel screening of a large number of potentially-infested stocks. We also have investigated several prophylactic measures to prevent the further contamination of stocks, namely UV-exposure, ethanol treatment, bleaching, and desiccation. Bleaching was found to kill all spores. Other treatments were less effective but were found to be sufficient to prevent further contamination of noninfested stocks. Two treatments were efficacious in curing infested stocks (1) bleaching of eggs and subsequent raising of the larvae in clean vials; (2) fumagillin treatment. These cures only work on stocks that have not become too weak to withstand the procedures.},
keywords = {Animals, Apansporoblastina, Apansporoblastina/*genetics/physiology, Base Sequence, cure, Disinfection, Disinfection/methods, DNA, DNA Primers, Drosophila melanogaster/*microbiology, ferrandon, fumagillin, Fungal, Fungal/chemistry, M3i, microsporidia, obligate intracellular parasitism, PCR detection, Phylogeny, Polymerase Chain Reaction, Polymerase Chain Reaction/methods, prophylaxis, Ribosomal, Ribosomal/chemistry, Sequence Alignment, Tubulinosema ratisbonensis},
pubstate = {published},
tppubtype = {article}
}
Benincasa Monica, Pacor Sabrina, Wu Wei, Prato Maurizio, Bianco Alberto, Gennaro Renato
Antifungal activity of amphotericin B conjugated to carbon nanotubes Journal Article
In: ACS nano, vol. 5, no. 1, pp. 199–208, 2011, ISSN: 1936-086X.
Abstract | Links | BibTeX | Tags: Amphotericin B, Antifungal Agents, Candida, carbon, Cell Membrane, Deoxycholic Acid, Drug Design, Drug Resistance, Fungal, Humans, I2CT, Jurkat Cells, Kinetics, Membrane Potentials, Nanotubes, Team-Bianco
@article{benincasa_antifungal_2011,
title = {Antifungal activity of amphotericin B conjugated to carbon nanotubes},
author = {Monica Benincasa and Sabrina Pacor and Wei Wu and Maurizio Prato and Alberto Bianco and Renato Gennaro},
doi = {10.1021/nn1023522},
issn = {1936-086X},
year = {2011},
date = {2011-01-01},
journal = {ACS nano},
volume = {5},
number = {1},
pages = {199--208},
abstract = {Amphotericin B (AMB) has long been considered the most effective drug in the treatment of serious invasive fungal infections. There are, however, major limitations to its use, due to several adverse effects, including acute infusional reactions and, most relevant, a dose-dependent nephrotoxicity. At least some of these effects are attributed to the aggregation of AMB as a result of its poor water solubility. To overcome this problem, reformulated versions of the drug have been developed, including a micellar dispersion of AMB with sodium deoxycholate (AMBD), its encapsulation into liposomes, or its incorporation into lipidic complexes. The development of nanobiotechnologies provides novel potential drug delivery systems that make use of nanomaterials such as functionalized carbon nanotubes (f-CNTs), which are emerging as an innovative and efficient tool for the transport and cellular translocation of therapeutic molecules. In this study, we prepared two conjugates between f-CNTs and AMB. The antifungal activity of these conjugates was tested against a collection of reference and clinical fungal strains, in comparison to that of AMB alone or AMBD. Measured minimum inhibition concentration (MIC) values for f-CNT-AMB conjugates were either comparable to or better than those displayed by AMB and AMBD. Furthermore, AMBD-resistant Candida strains were found to be susceptible to f-CNT-AMB 1. Additional studies, aimed at understanding the mechanism of action of the conjugates, suggest a nonlytic mechanism, since the compounds show a major permeabilizing effect on the tested fungal strains only after extended incubation. Interestingly, the f-CNT-AMB 1 does not show any significant toxic effect on Jurkat cells at antifungal concentrations.},
keywords = {Amphotericin B, Antifungal Agents, Candida, carbon, Cell Membrane, Deoxycholic Acid, Drug Design, Drug Resistance, Fungal, Humans, I2CT, Jurkat Cells, Kinetics, Membrane Potentials, Nanotubes, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Matskevich Alexey A, Quintin Jessica, Ferrandon Dominique
The Drosophila PRR GNBP3 assembles effector complexes involved in antifungal defenses independently of its Toll-pathway activation function Journal Article
In: Eur. J. Immunol., vol. 40, no. 5, pp. 1244–1254, 2010, ISSN: 1521-4141.
Abstract | Links | BibTeX | Tags: Agglutination, Animals, Beauveria, Beauveria/immunology, Candida albicans, Candida albicans/immunology, Carrier Proteins, Carrier Proteins/*immunology/pharmacology, Drosophila melanogaster/*immunology/microbiology, Drosophila Proteins/*immunology/pharmacology/physiology, Enzyme Activation, ferrandon, Fungal, Fungi, Fungi/*immunology, Hemolymph, Hemolymph/immunology, M3i, Melanins, Melanins/*physiology, Monophenol Monooxygenase, Monophenol Monooxygenase/physiology, Multiprotein Complexes, Multiprotein Complexes/physiology, Recombinant Fusion Proteins, Recombinant Fusion Proteins/pharmacology, Serpins, Serpins/physiology, Spores, Toll-Like Receptors, Toll-Like Receptors/immunology
@article{matskevich_drosophila_2010b,
title = {The Drosophila PRR GNBP3 assembles effector complexes involved in antifungal defenses independently of its Toll-pathway activation function},
author = {Alexey A Matskevich and Jessica Quintin and Dominique Ferrandon},
doi = {10.1002/eji.200940164},
issn = {1521-4141},
year = {2010},
date = {2010-05-01},
journal = {Eur. J. Immunol.},
volume = {40},
number = {5},
pages = {1244--1254},
abstract = {The Drosophila Toll-signaling pathway controls the systemic antifungal host response. Gram-negative binding protein 3 (GNBP3), a member of the beta-glucan recognition protein family senses fungal infections and activates this pathway. A second detection system perceives the activity of proteolytic fungal virulence factors and redundantly activates Toll. GNBP3(hades) mutant flies succumb more rapidly to Candida albicans and to entomopathogenic fungal infections than WT flies, despite normal triggering of the Toll pathway via the virulence detection system. These observations suggest that GNBP3 triggers antifungal defenses that are not dependent on activation of the Toll pathway. Here, we show that GNBP3 agglutinates fungal cells. Furthermore, it can activate melanization in a Toll-independent manner. Melanization is likely to be an essential defense against some fungal infections given that the entomopathogenic fungus Beauveria bassiana inhibits the activity of the main melanization enzymes, the phenol oxidases. Finally, we show that GNBP3 assembles "attack complexes", which comprise phenoloxidase and the necrotic serpin. We propose that Drosophila GNBP3 targets fungi immediately at the inception of the infection by bringing effector molecules in direct contact with the invading microorganisms.},
keywords = {Agglutination, Animals, Beauveria, Beauveria/immunology, Candida albicans, Candida albicans/immunology, Carrier Proteins, Carrier Proteins/*immunology/pharmacology, Drosophila melanogaster/*immunology/microbiology, Drosophila Proteins/*immunology/pharmacology/physiology, Enzyme Activation, ferrandon, Fungal, Fungi, Fungi/*immunology, Hemolymph, Hemolymph/immunology, M3i, Melanins, Melanins/*physiology, Monophenol Monooxygenase, Monophenol Monooxygenase/physiology, Multiprotein Complexes, Multiprotein Complexes/physiology, Recombinant Fusion Proteins, Recombinant Fusion Proteins/pharmacology, Serpins, Serpins/physiology, Spores, Toll-Like Receptors, Toll-Like Receptors/immunology},
pubstate = {published},
tppubtype = {article}
}
Roetzer Andreas, Gregori Christa, Jennings Ann Marie, Quintin Jessica, Ferrandon Dominique, Butler Geraldine, Kuchler Karl, Ammerer Gustav, Schüller Christoph
Candida glabrata environmental stress response involves Saccharomyces cerevisiae Msn2/4 orthologous transcription factors Journal Article
In: Mol. Microbiol., vol. 69, no. 3, pp. 603–620, 2008, ISSN: 1365-2958.
Abstract | Links | BibTeX | Tags: Animals, Candida glabrata, Candidiasis, DNA-Binding Proteins, ferrandon, Fungal, Fungal Proteins, Gene Expression Profiling, Gene Expression Regulation, Genetic, Humans, M3i, Oligonucleotide Array Sequence Analysis, Osmotic Pressure, Regulon, Saccharomyces cerevisiae Proteins, Transcription, Transcription Factors, Virulence, Yeasts
@article{roetzer_candida_2008b,
title = {Candida glabrata environmental stress response involves Saccharomyces cerevisiae Msn2/4 orthologous transcription factors},
author = {Andreas Roetzer and Christa Gregori and Ann Marie Jennings and Jessica Quintin and Dominique Ferrandon and Geraldine Butler and Karl Kuchler and Gustav Ammerer and Christoph Schüller},
doi = {10.1111/j.1365-2958.2008.06301.x},
issn = {1365-2958},
year = {2008},
date = {2008-01-01},
journal = {Mol. Microbiol.},
volume = {69},
number = {3},
pages = {603--620},
abstract = {We determined the genome-wide environmental stress response (ESR) expression profile of Candida glabrata, a human pathogen related to Saccharomyces cerevisiae. Despite different habitats, C. glabrata, S. cerevisiae, Schizosaccharomyces pombe and Candida albicans have a qualitatively similar ESR. We investigate the function of the C. glabrata syntenic orthologues to the ESR transcription factor Msn2. The C. glabrata orthologues CgMsn2 and CgMsn4 contain a motif previously referred to as HD1 (homology domain 1) also present in Msn2 orthologues from fungi closely related to S. cerevisiae. We show that regions including this motif confer stress-regulated intracellular localization when expressed in S. cerevisiae. Site-directed mutagenesis confirms that nuclear export of CgMsn2 in C. glabrata requires an intact HD1. Transcript profiles of CgMsn2/4 mutants and CgMsn2 overexpression strains show that they regulate a part of the CgESR. CgMsn2 complements a S. cerevisiae msn2 null mutant and in stressed C. glabrata cells, rapidly translocates from the cytosol to the nucleus. CgMsn2 is required for full resistance against severe osmotic stress and rapid and full induction of trehalose synthesis genes (TPS1, TPS2). Constitutive activation of CgMsn2 is detrimental for C. glabrata. These results establish an Msn2-regulated general stress response in C. glabrata.},
keywords = {Animals, Candida glabrata, Candidiasis, DNA-Binding Proteins, ferrandon, Fungal, Fungal Proteins, Gene Expression Profiling, Gene Expression Regulation, Genetic, Humans, M3i, Oligonucleotide Array Sequence Analysis, Osmotic Pressure, Regulon, Saccharomyces cerevisiae Proteins, Transcription, Transcription Factors, Virulence, Yeasts},
pubstate = {published},
tppubtype = {article}
}
Cristofari G., Bampi C., Wilhelm M., Wilhelm F. X., Darlix J. L.
A 5'-3' long-range interaction in Ty1 RNA controls its reverse transcription and retrotransposition Journal Article
In: EMBO J, vol. 21, no. 16, pp. 4368-79, 2002, (0261-4189 Journal Article).
Abstract | BibTeX | Tags: *Gene, *Transcription, Acid, cerevisiae/*genetics, Complementary/biosynthesis, Conformation, DNA, Expression, Fungal, Fungal/chemistry/*metabolism, Genetic, Gov't, in, Messenger/chemistry/*metabolism, Non-U.S., Nucleic, Phylogeny, Regulation, Retroelements/*genetics, RNA, Saccharomyces, Support, vitro
@article{,
title = {A 5'-3' long-range interaction in Ty1 RNA controls its reverse transcription and retrotransposition},
author = { G. Cristofari and C. Bampi and M. Wilhelm and F. X. Wilhelm and J. L. Darlix},
year = {2002},
date = {2002-01-01},
journal = {EMBO J},
volume = {21},
number = {16},
pages = {4368-79},
abstract = {LTR-retrotransposons are abundant components of all eukaryotic genomes and appear to be key players in their evolution. They share with retroviruses a reverse transcription step during their replication cycle. To better understand the replication of retrotransposons as well as their similarities to and differences from retroviruses, we set up an in vitro model system to examine minus-strand cDNA synthesis of the yeast Ty1 LTR-retrotransposon. Results show that the 5' and 3' ends of Ty1 genomic RNA interact through 14 nucleotide 5'-3' complementary sequences (CYC sequences). This 5'-3' base pairing results in an efficient initiation of reverse transcription in vitro. Transposition of a marked Ty1 element and Ty1 cDNA synthesis in yeast rely on the ability of the CYC sequences to base pair. This 5'-3' interaction is also supported by phylogenic analysis of all full-length Ty1 and Ty2 elements present in the Saccharomyces cerevisiae genome. These novel findings lead us to propose that circularization of the Ty1 genomic RNA controls initiation of reverse transcription and may limit reverse transcription of defective retroelements.},
note = {0261-4189
Journal Article},
keywords = {*Gene, *Transcription, Acid, cerevisiae/*genetics, Complementary/biosynthesis, Conformation, DNA, Expression, Fungal, Fungal/chemistry/*metabolism, Genetic, Gov't, in, Messenger/chemistry/*metabolism, Non-U.S., Nucleic, Phylogeny, Regulation, Retroelements/*genetics, RNA, Saccharomyces, Support, vitro},
pubstate = {published},
tppubtype = {article}
}
Adamkewicz J I, Mueller C G, Hansen K E, Prud'homme W A, Thorner J
Purification and enzymic properties of Mot1 ATPase, a regulator of basal transcription in the yeast Saccharomyces cerevisiae Journal Article
In: The Journal of Biological Chemistry, vol. 275, no. 28, pp. 21158–21168, 2000, ISSN: 0021-9258.
Abstract | Links | BibTeX | Tags: Adenosine Triphosphatases, Base Sequence, Chromatography, DNA Helicases, DNA-Binding Proteins, Fungal, Gel, Gene Expression Regulation, Genetic, Kinetics, Molecular Sequence Data, Molecular Weight, Osmolar Concentration, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, TATA Box, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Team-Mueller, Transcription, Transcription Factors
@article{adamkewicz_purification_2000,
title = {Purification and enzymic properties of Mot1 ATPase, a regulator of basal transcription in the yeast Saccharomyces cerevisiae},
author = {J I Adamkewicz and C G Mueller and K E Hansen and W A Prud'homme and J Thorner},
doi = {10.1074/jbc.M002639200},
issn = {0021-9258},
year = {2000},
date = {2000-07-01},
journal = {The Journal of Biological Chemistry},
volume = {275},
number = {28},
pages = {21158--21168},
abstract = {The 1867-residue Mot1 protein is a member of a superfamily of ATPases, some of which are helicases, that interact with protein-nucleic acid assemblies. Mot1 is an essential regulator of RNA polymerase II-dependent transcription in vivo and dissociates TATA box-binding protein (TBP)-DNA complexes in vitro. Mot1-(His)(6) was purified to apparent homogeneity from yeast extracts. The preparation efficiently dissociated TBP.TATA complexes, suggesting that no other protein or cofactor is required. Mot1 behaved as a non-globular monomer in hydrodynamic studies, and no association was detected between differentially tagged co-expressed Mot1 constructs. ATPase activity was stimulated about 10-fold by high ionic strength or alkaline pH, or by deletion of the N-terminal TBP-binding segment, suggesting that the N-terminal domain negatively regulates the C-terminal ATPase domain (Mot1C). Correspondingly, at moderate salt concentration, Mot1 ATPase (but not Mot1C) was stimulated textgreater/=10-fold by yeast TBP, suggesting that interaction with TBP relieves a conformational constraint in Mot1. Double- or single-stranded TATA-containing DNA did not affect ATPase activity of Mot1 or Mot1C, with or without TBP. Mot1 did not exhibit detectable helicase activity in strand displacement assays using substrates with flush ends or 5'- or 3'-overhangs. Mot1-catalyzed dissociation of TBP from DNA was not prevented by a psoralen cross-link positioned immediately preceding the TATA sequence. Thus, Mot1 most likely promotes release of TBP from TATA-containing DNA by causing a structural change in TBP itself, rather than by strand unwinding.},
keywords = {Adenosine Triphosphatases, Base Sequence, Chromatography, DNA Helicases, DNA-Binding Proteins, Fungal, Gel, Gene Expression Regulation, Genetic, Kinetics, Molecular Sequence Data, Molecular Weight, Osmolar Concentration, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, TATA Box, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Team-Mueller, Transcription, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
Rutschmann Sophie, Jung Alain C, Hetru Charles, Reichhart Jean-Marc, Hoffmann Jules A, Ferrandon Dominique
The Rel protein DIF mediates the antifungal but not the antibacterial host defense in Drosophila Journal Article
In: Immunity, vol. 12, no. 5, pp. 569–580, 2000, ISSN: 1074-7613.
Abstract | BibTeX | Tags: Animals, Antigens, Bacterial, DNA-Binding Proteins, ferrandon, Fungal, hoffmann, Immunity, Innate, M3i, reichhart, Transcription Factors
@article{rutschmann_rel_2000,
title = {The Rel protein DIF mediates the antifungal but not the antibacterial host defense in Drosophila},
author = {Sophie Rutschmann and Alain C Jung and Charles Hetru and Jean-Marc Reichhart and Jules A Hoffmann and Dominique Ferrandon},
issn = {1074-7613},
year = {2000},
date = {2000-05-01},
journal = {Immunity},
volume = {12},
number = {5},
pages = {569--580},
abstract = {We have isolated two Drosophila lines that carry point mutations in the gene coding for the NF-KB-like factor DIF. Like mutants of the Toll pathway, Dif mutant flies are susceptible to fungal but not to bacterial infections. Genetic epistasis experiments demonstrate that Dif mediates the Toll-dependent control of the inducibility of the antifungal peptide gene Drosomycin. Strikingly, DIF alone is required for the antifungal response in adults, but is redundant in larvae with Dorsal, another Rel family member. In Drosophila, Dif appears to be dedicated to the antifungal defense elicited by fungi and gram-positive bacteria. We discuss in this light the possibility that NF-KB1/p50 might be required more specifically in the innate immune response against gram-positive bacteria in mammals.},
keywords = {Animals, Antigens, Bacterial, DNA-Binding Proteins, ferrandon, Fungal, hoffmann, Immunity, Innate, M3i, reichhart, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
Braun A, Hoffmann Jules A, Meister Marie
Analysis of the Drosophila host defense in domino mutant larvae, which are devoid of hemocytes Journal Article
In: Proc. Natl. Acad. Sci. U.S.A., vol. 95, no. 24, pp. 14337–14342, 1998, ISSN: 0027-8424.
Abstract | BibTeX | Tags: Adipose Tissue, Animals, Candida, Escherichia coli, Fungal, Genotype, Hemocytes, hoffmann, Larva, M3i, Melanins, Micrococcus luteus, Spores
@article{braun_analysis_1998,
title = {Analysis of the Drosophila host defense in domino mutant larvae, which are devoid of hemocytes},
author = {A Braun and Jules A Hoffmann and Marie Meister},
issn = {0027-8424},
year = {1998},
date = {1998-11-01},
journal = {Proc. Natl. Acad. Sci. U.S.A.},
volume = {95},
number = {24},
pages = {14337--14342},
abstract = {We have analyzed the Drosophila immune response in domino mutant larvae, which are devoid of blood cells. The domino mutants have a good larval viability, but they die as prepupae. We show that, on immune challenge, induction of the genes encoding antimicrobial peptides in the fat body is not affected significantly in the mutant larvae, indicating that hemocytes are not essential in this process. The hemocoele of domino larvae contains numerous live microorganisms, the presence of which induces a weak antimicrobial response in the fat body. A full response is observed only after septic injury. We propose that the fat body cells are activated both by the presence of microorganisms and by injury and that injury potentiates the effect of microorganisms. Survival experiments after an immune challenge showed that domino mutants devoid of blood cells maintain a wild-type resistance to septic injury. This resistance was also observed in mutant larvae in which the synthesis of antibacterial peptides is impaired (immune deficiency larvae) and in mutants that are deficient for humoral melanization (Black cells larvae). However, if domino was combined with either the immune deficiency or the Black cell mutation, the resistance to septic injury was reduced severely. These results establish the relevance of the three immune reactions: phagocytosis, synthesis of antibacterial peptides, and melanization. By working in synergy, they provide Drosophila a highly effective defense against injury and/or infection.},
keywords = {Adipose Tissue, Animals, Candida, Escherichia coli, Fungal, Genotype, Hemocytes, hoffmann, Larva, M3i, Melanins, Micrococcus luteus, Spores},
pubstate = {published},
tppubtype = {article}
}
Ferrandon Dominique, Jung Alain C, Criqui M, Lemaitre Bruno, Uttenweiler-Joseph S, Michaut Lydia, Reichhart Jean-Marc, Hoffmann Jules A
A drosomycin-GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the Toll pathway Journal Article
In: EMBO J., vol. 17, no. 5, pp. 1217–1227, 1998, ISSN: 0261-4189.
Abstract | Links | BibTeX | Tags: Animals, bacteria, Cell Surface, Developmental, Digestive System, Epithelium, Fat Body, Female, ferrandon, Fungal, Gene Expression Regulation, Genes, Green Fluorescent Proteins, hoffmann, Insect Proteins, Larva, Luminescent Proteins, M3i, Male, Membrane Glycoproteins, Organ Specificity, Receptors, reichhart, Reporter, Respiratory System, Spores, Toll-Like Receptors, Trachea, Transgenes
@article{ferrandon_drosomycin-gfp_1998,
title = {A drosomycin-GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the Toll pathway},
author = {Dominique Ferrandon and Alain C Jung and M Criqui and Bruno Lemaitre and S Uttenweiler-Joseph and Lydia Michaut and Jean-Marc Reichhart and Jules A Hoffmann},
doi = {10.1093/emboj/17.5.1217},
issn = {0261-4189},
year = {1998},
date = {1998-08-01},
journal = {EMBO J.},
volume = {17},
number = {5},
pages = {1217--1227},
abstract = {A hallmark of the systemic antimicrobial response of Drosophila is the synthesis by the fat body of several antimicrobial peptides which are released into the hemolymph in response to a septic injury. One of these peptides, drosomycin, is active primarily against fungi. Using a drosomycin-green fluorescent protein (GFP) reporter gene, we now show that in addition to the fat body, a variety of epithelial tissues that are in direct contact with the external environment, including those of the respiratory, digestive and reproductive tracts, can express the antifungal peptide, suggesting a local response to infections affecting these barrier tissues. As is the case for vertebrate epithelia, insect epithelia appear to be more than passive physical barriers and are likely to constitute an active component of innate immunity. We also show that, in contrast to the systemic antifungal response, this local immune response is independent of the Toll pathway.},
keywords = {Animals, bacteria, Cell Surface, Developmental, Digestive System, Epithelium, Fat Body, Female, ferrandon, Fungal, Gene Expression Regulation, Genes, Green Fluorescent Proteins, hoffmann, Insect Proteins, Larva, Luminescent Proteins, M3i, Male, Membrane Glycoproteins, Organ Specificity, Receptors, reichhart, Reporter, Respiratory System, Spores, Toll-Like Receptors, Trachea, Transgenes},
pubstate = {published},
tppubtype = {article}
}
Motorin Y., Keith G., Simon C., Foiret D., Simos G., Hurt E., Grosjean H.
The yeast tRNA:pseudouridine synthase Pus1p displays a multisite substrate specificity Journal Article
In: RNA, vol. 4, no. 7, pp. 856-69, 1998, (1355-8382 Journal Article).
Abstract | BibTeX | Tags: *RNA, cerevisiae, Cloning, Fractions/metabolism, Fungal, Fungal/metabolism, Gov't, Hydro-Lyases/biosynthesis/genetics/*metabolism, Molecular, Mutation, Non-U.S., Plant/metabolism, post-transcriptional, Precursors/*metabolism, Processing, Proteins/biosynthesis, Proteins/biosynthesis/genetics/metabolism, Pseudouridine/*biosynthesis, Recombinant, RNA, Saccharomyces, Specificity, Subcellular, Substrate, Support, Transfer/*metabolism
@article{,
title = {The yeast tRNA:pseudouridine synthase Pus1p displays a multisite substrate specificity},
author = { Y. Motorin and G. Keith and C. Simon and D. Foiret and G. Simos and E. Hurt and H. Grosjean},
year = {1998},
date = {1998-01-01},
journal = {RNA},
volume = {4},
number = {7},
pages = {856-69},
abstract = {We have previously shown that the yeast gene PUS1 codes for a tRNA:pseudouridine synthase and that recombinant Pus1p catalyzes, in an intron-dependent way, the formation of psi34 and psi36 in the anticodon loop of the yeast minor tRNA(Ile) in vitro (Simos G et al., 1996, EMBO J 15:2270-2284). Using a set of T7 transcripts of different tRNA genes, we now demonstrate that yeast pseudouridine synthase 1 catalyzes in vitro pseudouridine formation at positions 27 and/or 28 in several yeast cytoplasmic tRNAs and at position 35 in the intron-containing tRNA(Tyr) (anticodon GUA). Thus, Pus1p not only displays a broad specificity toward the RNA substrates, but is also capable of catalyzing the pseudouridine (psi) formation at distinct noncontiguous sites within the same tRNA molecule. The cell-free extract prepared from the yeast strain bearing disrupted gene PUS1 is unable to catalyze the formation of psi27, psi28, psi34, and psi36 in vitro, however, psi35 formation in the intron-containing tRNA(Tyr)(GUA) remains unaffected. Thus, in yeast, only one gene product accounts for tRNA pseudouridylation at positions 27, 28, 34, and 36, whereas for position 35 in tRNA(Tyr), another site-specific tRNA:pseudouridine synthase with overlapping specificity exists. Mapping of pseudouridine residues present in various tRNAs extracted from the PUS1-disrupted strain confirms the in vitro data obtained with the recombinant Pus1p. In addition, they suggest that Pus1p is implicated in modification at positions U26, U65, and U67 in vivo.},
note = {1355-8382
Journal Article},
keywords = {*RNA, cerevisiae, Cloning, Fractions/metabolism, Fungal, Fungal/metabolism, Gov't, Hydro-Lyases/biosynthesis/genetics/*metabolism, Molecular, Mutation, Non-U.S., Plant/metabolism, post-transcriptional, Precursors/*metabolism, Processing, Proteins/biosynthesis, Proteins/biosynthesis/genetics/metabolism, Pseudouridine/*biosynthesis, Recombinant, RNA, Saccharomyces, Specificity, Subcellular, Substrate, Support, Transfer/*metabolism},
pubstate = {published},
tppubtype = {article}
}
Heyman T., Agoutin B., Friant S., Wilhelm F. X., Wilhelm M. L.
Plus-strand DNA synthesis of the yeast retrotransposon Ty1 is initiated at two sites, PPT1 next to the 3' LTR and PPT2 within the pol gene. PPT1 is sufficient for Ty1 transposition Journal Article
In: J Mol Biol, vol. 253, no. 2, pp. 291-303, 1995, (0022-2836 Journal Article).
Abstract | BibTeX | Tags: *DNA, *Genes, *Repetitive, *Retroelements, Acid, Base, C/analysis, cerevisiae/genetics/*virology, Chain, Cloning, Data, DNA, Fungal, Fungal/biosynthesis, Genes, Genetic, Genome, Gov't, Mapping, Molecular, Non-U.S., Nucleic, pol, Poly, Polymerase, Primers, Reaction, Replication, Restriction, Saccharomyces, Sequence, Sequences, Support, Transcription, Viral, Viral/*biosynthesis
@article{,
title = {Plus-strand DNA synthesis of the yeast retrotransposon Ty1 is initiated at two sites, PPT1 next to the 3' LTR and PPT2 within the pol gene. PPT1 is sufficient for Ty1 transposition},
author = { T. Heyman and B. Agoutin and S. Friant and F. X. Wilhelm and M. L. Wilhelm},
year = {1995},
date = {1995-01-01},
journal = {J Mol Biol},
volume = {253},
number = {2},
pages = {291-303},
abstract = {Long terminal repeat elements and retroviruses require primers for initiation of minus and plus-strand DNA synthesis by reverse transcriptase. Here we demonstrate genetically that plus-strand DNA synthesis of the yeast Ty1 element is initiated at two sites located at the 5' boundary of the 3' long terminal repeat (PPT1) and near the middle of the pol gene in the integrase coding sequence (PPT2). A consequence of the presence of two PPTs is that Ty1 plus-strand DNA exists as segments at some time during replication. Three fragments have been identified: the plus-strand strong-stop DNA initiated at PPT1, a downstream fragment initiated at PPT2 and an upstream fragment spanning the 5'-terminal part of Ty1 and a portion of the TyB gene. Characterization of the 3' ends of the plus-strand DNA fragments reveals (1) that the upstream fragment is elongated beyond PPT2 creating a plus-strand overlap and (2) that the majority of plus-strand strong-stop DNA fragments bear a copy of the minus-strand primer binding site in agreement with the accepted model of retroviral genomic RNA reverse transcription. The two polypurine tracts, PPT1 and PPT2, have an identical sequence GGGTGGTA. Mutations replacing purines by pyrimidines in this sequence significantly diminish or abolish initiation of plus-strand synthesis. Ty1 elements bearing a mutated PPT2 sequence are not defective for transposition whereas mutations in PPT1 abolish transposition.},
note = {0022-2836
Journal Article},
keywords = {*DNA, *Genes, *Repetitive, *Retroelements, Acid, Base, C/analysis, cerevisiae/genetics/*virology, Chain, Cloning, Data, DNA, Fungal, Fungal/biosynthesis, Genes, Genetic, Genome, Gov't, Mapping, Molecular, Non-U.S., Nucleic, pol, Poly, Polymerase, Primers, Reaction, Replication, Restriction, Saccharomyces, Sequence, Sequences, Support, Transcription, Viral, Viral/*biosynthesis},
pubstate = {published},
tppubtype = {article}
}
Auble D T, Hansen K E, Mueller C G, Lane W S, Thorner J, Hahn S
Mot1, a global repressor of RNA polymerase II transcription, inhibits TBP binding to DNA by an ATP-dependent mechanism Journal Article
In: Genes & Development, vol. 8, no. 16, pp. 1920–1934, 1994, ISSN: 0890-9369.
Abstract | Links | BibTeX | Tags: Adenosine Triphosphatases, Adenosine Triphosphate, Amino Acid Sequence, Base Sequence, Biological, DNA, DNA Helicases, DNA Probes, DNA-Binding Proteins, Fungal, Fungal Proteins, Genes, Genetic, Models, Molecular Sequence Data, Mutagenesis, Repressor Proteins, RNA Polymerase II, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Site-Directed, TATA Box, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Team-Mueller, Transcription, Transcription Factors
@article{auble_mot1_1994,
title = {Mot1, a global repressor of RNA polymerase II transcription, inhibits TBP binding to DNA by an ATP-dependent mechanism},
author = {D T Auble and K E Hansen and C G Mueller and W S Lane and J Thorner and S Hahn},
doi = {10.1101/gad.8.16.1920},
issn = {0890-9369},
year = {1994},
date = {1994-08-01},
journal = {Genes & Development},
volume = {8},
number = {16},
pages = {1920--1934},
abstract = {Basal transcription of many genes in yeast is repressed by Mot1, an essential protein which is a member of the Snf2/Swi2 family of conserved nuclear factors. ADI is an ATP-dependent inhibitor of TATA-binding protein (TBP) binding to DNA that inhibits transcription in vitro. Here we demonstrate that ADI is encoded by the MOT1 gene. Mutation of MOT1 abolishes ADI activity and derepresses basal transcription in vitro and in vivo. Recombinant Mot1 removes TBP from DNA and Mot1 contains an ATPase activity which is essential for its function. Genetic interactions between Mot1 and TBP indicate that their functions are interlinked in vivo. These results provide a general model for understanding the mechanism of action of a large family of nuclear factors involved in processes such as transcription and DNA repair.},
keywords = {Adenosine Triphosphatases, Adenosine Triphosphate, Amino Acid Sequence, Base Sequence, Biological, DNA, DNA Helicases, DNA Probes, DNA-Binding Proteins, Fungal, Fungal Proteins, Genes, Genetic, Models, Molecular Sequence Data, Mutagenesis, Repressor Proteins, RNA Polymerase II, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Site-Directed, TATA Box, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Team-Mueller, Transcription, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
Santos M. A., el-Adlouni C., Cox A. D., Luz J. M., Keith G., Tuite M. F.
Transfer RNA profiling: a new method for the identification of pathogenic Candida species Journal Article
In: Yeast, vol. 10, no. 5, pp. 625-36, 1994, (0749-503x Journal Article).
Abstract | BibTeX | Tags: Candida/classification/*genetics/pathogenicity, Electrophoresis, Fungal, Gel, Genetic, Gov't, Markers, Non-U.S., Polyacrylamide, RNA, Support, Transfer/*analysis
@article{,
title = {Transfer RNA profiling: a new method for the identification of pathogenic Candida species},
author = { M. A. Santos and C. el-Adlouni and A. D. Cox and J. M. Luz and G. Keith and M. F. Tuite},
year = {1994},
date = {1994-01-01},
journal = {Yeast},
volume = {10},
number = {5},
pages = {625-36},
abstract = {A new molecular taxonomic method applicable to the identification of medically important Candida species and other yeast species has been developed. It is based on the electrophoretic pattern of total tRNA samples (a 'tRNA profile') isolated from Candida species and generated using high-resolution semi-denaturing urea-polyacrylamide gel electrophoresis and methylene blue staining. Species-specific tRNA profiles for the species C. albicans, C. tropicalis, C. parapsilosis, C. guilliermondii, C. glabrata and Pichia guilliermondii were obtained. Detailed studies with the major human pathogen of the Candida genus, C. albicans, demonstrated that the tRNA profile for a given species was both reproducible and strain-independent; seven different C. albicans strains generated identical tRNA profiles. Minor strain-specific heterogeneities in the tRNA profiles of C. guilliermondii and C. parapsilosis were detected, but in neither case did they significantly alter the species-specific diagnostic tRNA profile. The potential of this method in clarifying taxonomic anomalies was demonstrated by the finding that Type I and Type II strains of C. stellatoidea generate very different tRNA profiles, with that of a Type II strain being identical to the C. albicans tRNA profile. This method offers a number of advantages over current electrophoretic karyotype methods for species identification, both within the Candida genus and with yeast species in general.},
note = {0749-503x
Journal Article},
keywords = {Candida/classification/*genetics/pathogenicity, Electrophoresis, Fungal, Gel, Genetic, Gov't, Markers, Non-U.S., Polyacrylamide, RNA, Support, Transfer/*analysis},
pubstate = {published},
tppubtype = {article}
}
Wilhelm M. L., Reinbolt J., Gangloff J., Dirheimer G., Wilhelm F. X.
Transfer RNA binding protein in the nucleus of Saccharomyces cerevisiae Journal Article
In: FEBS Lett, vol. 349, no. 2, pp. 260-4, 1994, (0014-5793 Journal Article).
Abstract | BibTeX | Tags: *Saccharomyces, &, Acid, Amino, Cell, cerevisiae, cerevisiae/*metabolism, Chromatography, Data, DNA-Binding, DNA/metabolism, Fungal, Fungal/*isolation, high, liquid, Molecular, Nucleus/*metabolism, Pressure, Proteins, Proteins/genetics/*metabolism, purification, RNA, Saccharomyces, Sequence, Transfer/*isolation
@article{,
title = {Transfer RNA binding protein in the nucleus of Saccharomyces cerevisiae},
author = { M. L. Wilhelm and J. Reinbolt and J. Gangloff and G. Dirheimer and F. X. Wilhelm},
year = {1994},
date = {1994-01-01},
journal = {FEBS Lett},
volume = {349},
number = {2},
pages = {260-4},
abstract = {A yeast nuclear protein that binds to tRNA was identified using a RNA mobility shift assay. Northwestern blotting and N-terminal sequencing experiments indicate that this tRNA-binding protein is identical to zuotin which has previously been shown to bind to Z-DNA [(1992) EMBO J. 11, 3787-3796]. Labeled tRNA and poly(dG-m5dC) stabilized in the Z-DNA form identify the same protein on a Northwestern blot. In a gel retardation assay poly(dG-m5dC) in the Z-form strongly diminishes the binding of tRNA to zuotin. These studies establish that zuotin is able to bind to both tRNA and Z-DNA. Zuotin may be transiently associated with tRNA in the nucleus of yeast cells and play a role in its processing or transport to the cytoplasm.},
note = {0014-5793
Journal Article},
keywords = {*Saccharomyces, &, Acid, Amino, Cell, cerevisiae, cerevisiae/*metabolism, Chromatography, Data, DNA-Binding, DNA/metabolism, Fungal, Fungal/*isolation, high, liquid, Molecular, Nucleus/*metabolism, Pressure, Proteins, Proteins/genetics/*metabolism, purification, RNA, Saccharomyces, Sequence, Transfer/*isolation},
pubstate = {published},
tppubtype = {article}
}
Santos M. A., Keith G., Tuite M. F.
Non-standard translational events in Candida albicans mediated by an unusual seryl-tRNA with a 5'-CAG-3' (leucine) anticodon Journal Article
In: EMBO J, vol. 12, no. 2, pp. 607-16, 1993, (0261-4189 Journal Article).
Abstract | BibTeX | Tags: *Anticodon, *Translation, &, Acid, albicans/*genetics, Base, Candida, Cloning, Conformation, Data, DNA, Fungal, Fungal/chemistry/genetics/isolation, Genes, Genetic, Gov't, Leucine/*genetics, Molecular, Non-U.S., Nucleic, purification, RNA, Sequence, Ser/chemistry/*genetics/isolation, Support, Transfer
@article{,
title = {Non-standard translational events in Candida albicans mediated by an unusual seryl-tRNA with a 5'-CAG-3' (leucine) anticodon},
author = { M. A. Santos and G. Keith and M. F. Tuite},
year = {1993},
date = {1993-01-01},
journal = {EMBO J},
volume = {12},
number = {2},
pages = {607-16},
abstract = {From in vitro translation studies we have previously demonstrated the existence of an apparent efficient UAG (amber) suppressor tRNA in the dimorphic fungus Candida albicans (Santos et al., 1990). Using an in vitro assay for termination codon readthrough the tRNA responsible was purified to homogeneity from C.albicans cells. The determined sequence of the purified tRNA predicts a 5'-CAG-3' anticodon that should decode the leucine codon CUG and not the UAG termination codon as originally hypothesized. However, the tRNA(CAG) sequence shows greater nucleotide homology with seryl-tRNAs from the closely related yeast Saccharomyces cerevisiae than with leucyl-tRNAs from the same species. In vitro tRNA-charging studies demonstrated that the purified tRNA(CAG) is charged with Ser. The gene encoding the tRNA was cloned from C.albicans by a PCR-based strategy and DNA sequence analysis confirmed both the structure of the tRNA(CAG) and the absence of any introns in the tRNA gene. The copy number of the tRNA(CAG) gene (1-2 genes per haploid genome) is in agreement with the relatively low abundance (< 0.5% total tRNA) of this tRNA. In vitro translation studies revealed that the purified tRNA(CAG) could induce apparent translational bypass of all three termination codons. However, peptide mapping of in vitro translation products demonstrated that the tRNA(CAG) induces translational misreading in the amino-terminal region of two RNA templates employed, namely the rabbit alpha- and beta-globin mRNAs. These results suggest that the C.albicans tRNA(CAG) is not an 'omnipotent' suppressor tRNA but rather may mediate a novel non-standard translational event in vitro during the translation of the CUG codon. The possible nature of this non-standard translation event is discussed in the context of both the unusual structural features of the tRNA(CAG) and its in vitro behaviour.},
note = {0261-4189
Journal Article},
keywords = {*Anticodon, *Translation, &, Acid, albicans/*genetics, Base, Candida, Cloning, Conformation, Data, DNA, Fungal, Fungal/chemistry/genetics/isolation, Genes, Genetic, Gov't, Leucine/*genetics, Molecular, Non-U.S., Nucleic, purification, RNA, Sequence, Ser/chemistry/*genetics/isolation, Support, Transfer},
pubstate = {published},
tppubtype = {article}
}
Glasser A. L., el Adlouni C., Keith G., Sochacka E., Malkiewicz A., Santos M., Tuite M. F., Desgres J.
Presence and coding properties of 2'-O-methyl-5-carbamoylmethyluridine (ncm5Um) in the wobble position of the anticodon of tRNA(Leu) (U*AA) from brewer's yeast Journal Article
In: FEBS Lett, vol. 314, no. 3, pp. 381-5, 1992, (0014-5793 Journal Article).
Abstract | BibTeX | Tags: *Anticodon, &, Analysis, cerevisiae/*genetics, Chromatography, derivatives/analysis/chemistry/genetics, Fungal, Fungal/genetics, Gov't, high, Leu/*genetics, liquid, Mass, Molecular, Non-U.S., Pressure, Proteins/biosynthesis, RNA, Saccharomyces, Spectrophotometry, Spectrum, structure, Support, Transfer, Ultraviolet, Uridine/*analogs
@article{,
title = {Presence and coding properties of 2'-O-methyl-5-carbamoylmethyluridine (ncm5Um) in the wobble position of the anticodon of tRNA(Leu) (U*AA) from brewer's yeast},
author = { A. L. Glasser and C. el Adlouni and G. Keith and E. Sochacka and A. Malkiewicz and M. Santos and M. F. Tuite and J. Desgres},
year = {1992},
date = {1992-01-01},
journal = {FEBS Lett},
volume = {314},
number = {3},
pages = {381-5},
abstract = {The unknown modified nucleoside U* has been isolated by enzymatic and HPLC protocols from tRNA(Leu) (U*AA) recently discovered in brewer's yeast. The pure U* nucleoside has been characterized by electron impact mass spectroscopy, and comparison of its chromatographic and UV-absorption properties with those of appropriate synthetic compounds. The structure of U* was established as 2'-O-methyl-5-carbamoylmethyluridine (ncm5Um). The yeast tRNA(Leu) (U*AA) is the only tRNA so far sequenced which has been shown to contain ncm5Um. The location of such a modified uridine at the first position of the anticodon restricts the decoding property to A of the leucine UUA codon.},
note = {0014-5793
Journal Article},
keywords = {*Anticodon, &, Analysis, cerevisiae/*genetics, Chromatography, derivatives/analysis/chemistry/genetics, Fungal, Fungal/genetics, Gov't, high, Leu/*genetics, liquid, Mass, Molecular, Non-U.S., Pressure, Proteins/biosynthesis, RNA, Saccharomyces, Spectrophotometry, Spectrum, structure, Support, Transfer, Ultraviolet, Uridine/*analogs},
pubstate = {published},
tppubtype = {article}
}
Mueller C G, Nordheim A
A protein domain conserved between yeast MCM1 and human SRF directs ternary complex formation Journal Article
In: The EMBO journal, vol. 10, no. 13, pp. 4219–4229, 1991, ISSN: 0261-4189.
Abstract | BibTeX | Tags: Amino Acid Sequence, Base Sequence, DNA, DNA-Binding Proteins, Fungal, Fungal Proteins, Humans, Minichromosome Maintenance 1 Protein, Molecular Sequence Data, Nuclear Proteins, Nucleic Acid, Plasmids, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Serum Response Factor, Team-Mueller, Transcription Factors
@article{mueller_protein_1991,
title = {A protein domain conserved between yeast MCM1 and human SRF directs ternary complex formation},
author = {C G Mueller and A Nordheim},
issn = {0261-4189},
year = {1991},
date = {1991-12-01},
journal = {The EMBO journal},
volume = {10},
number = {13},
pages = {4219--4229},
abstract = {MCM1 and SRF bind to the same DNA sequence and form ternary complexes with STE12 and p62TCF, respectively. We show that in gel retardation assays, MCM1 recruits both ternary complex factors whereas SRF interacts only with p62TCF. A protein domain of 90 amino acids, shared by MCM1 and SRF, was found to be sufficient for ternary complex formation. The domain is also required for dimerization and DNA binding. Similar regions are found in other proteins, such as ARG80, Deficiens and Agamous. ARG80 and Agamous exhibit similar DNA binding specificities but do not interact with either STE12 or p62TCF. By exchanging three residues of ARG80 with those of corresponding positions in SRF (residues 198, 200 and 203), the ARG80 protein acquires the ability to recruit p62TCF into a ternary complex. Likewise, the substitution of four SRF amino acids by MCM1-derived residues (amino acids 73, 75, 77 and 78) confers on SRF the ability to interact with STE12. Thus, we have identified specific amino acids in MCM1 and SRF that are critical for ternary complex formation and which map to equivalent positions within the shared domains. Therefore, the structural basis for specific protein-protein interaction appears to be conserved in evolution between a class of transcription factors.},
keywords = {Amino Acid Sequence, Base Sequence, DNA, DNA-Binding Proteins, Fungal, Fungal Proteins, Humans, Minichromosome Maintenance 1 Protein, Molecular Sequence Data, Nuclear Proteins, Nucleic Acid, Plasmids, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Homology, Serum Response Factor, Team-Mueller, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}