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2000
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}
}
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.
1996
Charlet Maurice, Chernysh S, Philippe H, Hetru Charles, Hoffmann Jules A, Bulet Philippe
Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis Journal Article
In: J. Biol. Chem., vol. 271, no. 36, pp. 21808–21813, 1996, ISSN: 0021-9258.
Abstract | BibTeX | Tags: Amino Acid, Animals, Anti-Infective Agents, Antifungal Agents, Bivalvia, Blood Proteins, Chromatography, Cysteine, Defensins, High Pressure Liquid, hoffmann, M3i, Molecular Weight, Phylogeny, Sequence Homology
@article{charlet_innate_1996,
title = {Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis},
author = {Maurice Charlet and S Chernysh and H Philippe and Charles Hetru and Jules A Hoffmann and Philippe Bulet},
issn = {0021-9258},
year = {1996},
date = {1996-09-01},
journal = {J. Biol. Chem.},
volume = {271},
number = {36},
pages = {21808--21813},
abstract = {We have isolated from the blood of immune-challenged and untreated mussels (Mytilus edulis) antibacterial and antifungal peptides. We have characterized two isoforms of a novel 34-residue, cysteine-rich, peptide with potent bactericidal activity and partially characterized a novel 6.2-kDa antifungal peptide containing 12 cysteines. We report the presence of two members of the insect defensin family of antibacterial peptides and provide a phylogenetic analysis that indicates that mollusc and arthropod defensins have a common ancestry. Our data argue that circulating antimicrobial peptides represent an ancient host defense mechanism that predated the separation between molluscs and arthropods at the root of the Cambrian, about 545 million years ago.},
keywords = {Amino Acid, Animals, Anti-Infective Agents, Antifungal Agents, Bivalvia, Blood Proteins, Chromatography, Cysteine, Defensins, High Pressure Liquid, hoffmann, M3i, Molecular Weight, Phylogeny, Sequence Homology},
pubstate = {published},
tppubtype = {article}
}
We have isolated from the blood of immune-challenged and untreated mussels (Mytilus edulis) antibacterial and antifungal peptides. We have characterized two isoforms of a novel 34-residue, cysteine-rich, peptide with potent bactericidal activity and partially characterized a novel 6.2-kDa antifungal peptide containing 12 cysteines. We report the presence of two members of the insect defensin family of antibacterial peptides and provide a phylogenetic analysis that indicates that mollusc and arthropod defensins have a common ancestry. Our data argue that circulating antimicrobial peptides represent an ancient host defense mechanism that predated the separation between molluscs and arthropods at the root of the Cambrian, about 545 million years ago.
1981
Lagueux Marie, Harry P, Hoffmann Jules A
Ecdysteroids are bound to vitellin in newly laid eggs of Locusta Journal Article
In: Mol. Cell. Endocrinol., vol. 24, no. 3, pp. 325–338, 1981, ISSN: 0303-7207.
Abstract | BibTeX | Tags: Animals, Chromatography, Ecdysteroids, Female, Grasshoppers, High Pressure Liquid, hoffmann, Invertebrate Hormones, Lipoproteins, M3i, Molecular Weight, Ovum, Peptide Hydrolases, Radioimmunoassay, Vitellogenins
@article{lagueux_ecdysteroids_1981,
title = {Ecdysteroids are bound to vitellin in newly laid eggs of Locusta},
author = {Marie Lagueux and P Harry and Jules A Hoffmann},
issn = {0303-7207},
year = {1981},
date = {1981-12-01},
journal = {Mol. Cell. Endocrinol.},
volume = {24},
number = {3},
pages = {325--338},
abstract = {The follicle cells of vitellogenic ovaries of Locusta migratoria have been reported to synthesize impressive amounts of ecdysteroids which accumulate inside the oöcytes where they persist during egg-laying; these ecdysteroids are conjugated to more than 95%, and it is believed that their hydrolysis in the egg is the source of the peaks of free ecdysone observed in early embryonic development. The present paper shows that, in the eggs, the ecdysteroid conjugates are bound to a 520 000-dalton macromolecule which shares several characteristics with the major yolk protein vitellin and is precipitated by an anti-vitellin antibody. The physiological relevance of the binding of ovarian ecdysteroid conjugates is discussed in respect to the transfer of maternal ecdysteroids to the embryo.},
keywords = {Animals, Chromatography, Ecdysteroids, Female, Grasshoppers, High Pressure Liquid, hoffmann, Invertebrate Hormones, Lipoproteins, M3i, Molecular Weight, Ovum, Peptide Hydrolases, Radioimmunoassay, Vitellogenins},
pubstate = {published},
tppubtype = {article}
}
The follicle cells of vitellogenic ovaries of Locusta migratoria have been reported to synthesize impressive amounts of ecdysteroids which accumulate inside the oöcytes where they persist during egg-laying; these ecdysteroids are conjugated to more than 95%, and it is believed that their hydrolysis in the egg is the source of the peaks of free ecdysone observed in early embryonic development. The present paper shows that, in the eggs, the ecdysteroid conjugates are bound to a 520 000-dalton macromolecule which shares several characteristics with the major yolk protein vitellin and is precipitated by an anti-vitellin antibody. The physiological relevance of the binding of ovarian ecdysteroid conjugates is discussed in respect to the transfer of maternal ecdysteroids to the embryo.
