Publications
2021
Scheer Hélène, Almeida Caroline, Ferrier Emilie, Simonnot Quentin, Poirier Laure, Pflieger David, Sement François M., Koechler Sandrine, Piermaria Christina, Krawczyk Paweł, Mroczek Seweryn, Chicher Johana, Kuhn Lauriane, Dziembowski Andrzej, Hammann Philippe, Zuber Hélène, Gagliardi Dominique
The TUTase URT1 connects decapping activators and prevents the accumulation of excessively deadenylated mRNAs to avoid siRNA biogenesis Article de journal
Dans: Nature Communications, vol. 12, no. 1, p. 1298, 2021, ISSN: 2041-1723.
Résumé | Liens | BibTeX | Étiquettes: Arabidopsis, Arabidopsis Proteins, Co-Repressor Proteins, DEAD-box RNA Helicases, Gene Expression Regulation, Humans, messenger, Plant, PPSE, Proto-Oncogene Proteins, Ribonucleoproteins, RNA, RNA Nucleotidyltransferases, RNA Stability, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Small Interfering, Tobacco, transcriptome, Uridine
@article{scheer_tutase_2021,
title = {The TUTase URT1 connects decapping activators and prevents the accumulation of excessively deadenylated mRNAs to avoid siRNA biogenesis},
author = {Hélène Scheer and Caroline Almeida and Emilie Ferrier and Quentin Simonnot and Laure Poirier and David Pflieger and François M. Sement and Sandrine Koechler and Christina Piermaria and Paweł Krawczyk and Seweryn Mroczek and Johana Chicher and Lauriane Kuhn and Andrzej Dziembowski and Philippe Hammann and Hélène Zuber and Dominique Gagliardi},
doi = {10.1038/s41467-021-21382-2},
issn = {2041-1723},
year = {2021},
date = {2021-02-01},
journal = {Nature Communications},
volume = {12},
number = {1},
pages = {1298},
abstract = {Uridylation is a widespread modification destabilizing eukaryotic mRNAs. Yet, molecular mechanisms underlying TUTase-mediated mRNA degradation remain mostly unresolved. Here, we report that the Arabidopsis TUTase URT1 participates in a molecular network connecting several translational repressors/decapping activators. URT1 directly interacts with DECAPPING 5 (DCP5), the Arabidopsis ortholog of human LSM14 and yeast Scd6, and this interaction connects URT1 to additional decay factors like DDX6/Dhh1-like RNA helicases. Nanopore direct RNA sequencing reveals a global role of URT1 in shaping poly(A) tail length, notably by preventing the accumulation of excessively deadenylated mRNAs. Based on in vitro and in planta data, we propose a model that explains how URT1 could reduce the accumulation of oligo(A)-tailed mRNAs both by favoring their degradation and because 3' terminal uridines intrinsically hinder deadenylation. Importantly, preventing the accumulation of excessively deadenylated mRNAs avoids the biogenesis of illegitimate siRNAs that silence endogenous mRNAs and perturb Arabidopsis growth and development.},
keywords = {Arabidopsis, Arabidopsis Proteins, Co-Repressor Proteins, DEAD-box RNA Helicases, Gene Expression Regulation, Humans, messenger, Plant, PPSE, Proto-Oncogene Proteins, Ribonucleoproteins, RNA, RNA Nucleotidyltransferases, RNA Stability, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Small Interfering, Tobacco, transcriptome, Uridine},
pubstate = {published},
tppubtype = {article}
}
1998
Nicolas E, Reichhart Jean-Marc, Hoffmann Jules A, Lemaitre Bruno
In vivo regulation of the IkappaB homologue cactus during the immune response of Drosophila Article de journal
Dans: J. Biol. Chem., vol. 273, no. 17, p. 10463–10469, 1998, ISSN: 0021-9258.
Résumé | BibTeX | Étiquettes: Animals, Cell Surface, DNA-Binding Proteins, Gene Expression Regulation, hoffmann, Insect Proteins, Larva, M3i, Membrane Glycoproteins, Phosphoproteins, Proto-Oncogene Proteins, Receptors, reichhart, Signal Transduction, Toll-Like Receptors, Transcription Factor RelB, Transcription Factors
@article{nicolas_vivo_1998,
title = {In vivo regulation of the IkappaB homologue cactus during the immune response of Drosophila},
author = {E Nicolas and Jean-Marc Reichhart and Jules A Hoffmann and Bruno Lemaitre},
issn = {0021-9258},
year = {1998},
date = {1998-04-01},
journal = {J. Biol. Chem.},
volume = {273},
number = {17},
pages = {10463--10469},
abstract = {The dorsoventral regulatory gene pathway (spätzle/Toll/cactus) controls the expression of several antimicrobial genes during the immune response of Drosophila. This regulatory cascade shows striking similarities with the cytokine-induced activation cascade of NF-kappaB during the inflammatory response in mammals. Here, we have studied the regulation of the IkappaB homologue Cactus in the fat body during the immune response. We observe that the cactus gene is up-regulated in response to immune challenge. Interestingly, the expression of the cactus gene is controlled by the spätzle/Toll/cactus gene pathway, indicating that the cactus gene is autoregulated. We also show that two Cactus isoforms are expressed in the cytoplasm of fat body cells and that they are rapidly degraded and resynthesized after immune challenge. This degradation is also dependent on the Toll signaling pathway. Altogether, our results underline the striking similarities between the regulation of IkappaB and cactus during the immune response.},
keywords = {Animals, Cell Surface, DNA-Binding Proteins, Gene Expression Regulation, hoffmann, Insect Proteins, Larva, M3i, Membrane Glycoproteins, Phosphoproteins, Proto-Oncogene Proteins, Receptors, reichhart, Signal Transduction, Toll-Like Receptors, Transcription Factor RelB, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}
1996
Barillas-Mury Carolina, Charlesworth A, Gross I, Richman A, Hoffmann Jules A, Kafatos Fotis C
Immune factor Gambif1, a new rel family member from the human malaria vector, Anopheles gambiae Article de journal
Dans: EMBO J., vol. 15, no. 17, p. 4691–4701, 1996, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Amino Acid, Animals, Anopheles, Base Sequence, Biological Transport, Cell Nucleus, Cells, Complementary, Cultured, DNA, DNA-Binding Proteins, hoffmann, Insect Proteins, Insect Vectors, M3i, NF-kappa B, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-rel, Sequence Homology, Trans-Activators, Transcriptional Activation
@article{barillas-mury_immune_1996,
title = {Immune factor Gambif1, a new rel family member from the human malaria vector, Anopheles gambiae},
author = {Carolina Barillas-Mury and A Charlesworth and I Gross and A Richman and Jules A Hoffmann and Fotis C Kafatos},
issn = {0261-4189},
year = {1996},
date = {1996-09-01},
journal = {EMBO J.},
volume = {15},
number = {17},
pages = {4691--4701},
abstract = {A novel rel family member, Gambif1 (gambiae immune factor 1), has been cloned from the human malaria vector, Anopheles gambiae, and shown to be most similar to Drosophila Dorsal and Dif. Gambif1 protein is translocated to the nucleus in fat body cells in response to bacterial challenge, although the mRNA is present at low levels at all developmental stages and is not induced by infection. DNA binding activity to the kappaB-like sites in the A.gambiae Defensin and the Drosophila Diptericin and Cecropin promoters is also induced in larval nuclear extracts following infection. Gambif1 has the ability to bind to kappaB-like sites in vitro. Co-transfection assays in Drosophila mbn-2 cells show that Gambif1 can activate transcription by interacting with the Drosophila Diptericin regulatory elements, but is not functionally equivalent to Dorsal in this assay. Gambif1 protein translocation to the nucleus and the appearance of kappaB-like DNA binding activity can serve as molecular markers of activation of the immune system and open up the possibility of studying the role of defence reactions in determining mosquito susceptibility/refractoriness to malaria infection.},
keywords = {Amino Acid, Animals, Anopheles, Base Sequence, Biological Transport, Cell Nucleus, Cells, Complementary, Cultured, DNA, DNA-Binding Proteins, hoffmann, Insect Proteins, Insect Vectors, M3i, NF-kappa B, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-rel, Sequence Homology, Trans-Activators, Transcriptional Activation},
pubstate = {published},
tppubtype = {article}
}
1991
Hipskind R A, Rao V N, Mueller C G, Reddy E S, Nordheim A
Ets-related protein Elk-1 is homologous to the c-fos regulatory factor p62TCF Article de journal
Dans: Nature, vol. 354, no. 6354, p. 531–534, 1991, ISSN: 0028-0836.
Résumé | Liens | BibTeX | Étiquettes: Animals, Antibodies, Base Sequence, Binding Sites, DNA, DNA-Binding Proteins, Epitopes, Escherichia coli, ets-Domain Protein Elk-1, fos, Genes, Genetic, Immune Sera, Macromolecular Substances, Molecular Sequence Data, Mutagenesis, Nucleic Acid, Oligodeoxyribonucleotides, Oncogenic, Promoter Regions, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-ets, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Retroviridae Proteins, Saccharomyces cerevisiae, Sequence Homology, Site-Directed, Team-Mueller, Transcription Factors, Transfection
@article{hipskind_ets-related_1991,
title = {Ets-related protein Elk-1 is homologous to the c-fos regulatory factor p62TCF},
author = {R A Hipskind and V N Rao and C G Mueller and E S Reddy and A Nordheim},
doi = {10.1038/354531a0},
issn = {0028-0836},
year = {1991},
date = {1991-12-01},
journal = {Nature},
volume = {354},
number = {6354},
pages = {531--534},
abstract = {A key event in the response of cells to proliferative signals is the rapid, transient induction of the c-fos proto-oncogene, which is mediated through the serum response element (SRE) in the fos promoter. Genomic footprinting and transfection experiments suggest that this activation occurs through a ternary complex that includes the serum response factor (SRF) and the ternary complex factor p62. Interaction of p62TCF with the SRF-SRE binary complex requires a CAGGA tract immediately upstream of the SRE. Proteins of the ets proto-oncogene family bind to similar sequences and we have found that a member of this family, Elk-1, forms SRF-dependent ternary complexes with the SRE. Elk-1 and p62TCF have the same DNA sequence requirements and antibodies against Elk-1 block the binding of both proteins. Furthermore, we show that like p62TCF, Elk-1 forms complexes with the yeast SRF-homologue MCM1 but not with yeast ARG80. But ARG80 mutants that convey interaction with p62TCF can also form complexes with Elk-1. The similarity, or even identity, between Elk-1 and p62TCF suggests a novel regulatory role for Ets proteins that is effected through interaction with other proteins, such as SRF. Furthermore, the possible involvement of an Ets protein in the control of c-fos has interesting implications for proto-oncogene cooperation in cellular growth control.},
keywords = {Animals, Antibodies, Base Sequence, Binding Sites, DNA, DNA-Binding Proteins, Epitopes, Escherichia coli, ets-Domain Protein Elk-1, fos, Genes, Genetic, Immune Sera, Macromolecular Substances, Molecular Sequence Data, Mutagenesis, Nucleic Acid, Oligodeoxyribonucleotides, Oncogenic, Promoter Regions, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-ets, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Retroviridae Proteins, Saccharomyces cerevisiae, Sequence Homology, Site-Directed, Team-Mueller, Transcription Factors, Transfection},
pubstate = {published},
tppubtype = {article}
}
1990
Schröter H, Mueller C G, Meese K, Nordheim A
Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element Article de journal
Dans: The EMBO journal, vol. 9, no. 4, p. 1123–1130, 1990, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Base Sequence, Chloroquine, Gene Expression Regulation, Genetic, Glycosylation, HeLa Cells, Humans, Kinetics, Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Oligonucleotide Probes, Plasmids, Polymerase Chain Reaction, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Serum Response Factor, Team-Mueller, Transcription, Transcription Factors
@article{schroter_synergism_1990,
title = {Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element},
author = {H Schröter and C G Mueller and K Meese and A Nordheim},
issn = {0261-4189},
year = {1990},
date = {1990-04-01},
journal = {The EMBO journal},
volume = {9},
number = {4},
pages = {1123--1130},
abstract = {Transcriptional regulation of the c-fos proto-oncogene requires the serum response element (SRE) which is complexed by a multi-protein assembly observed both in vitro and in vivo. Two protein factors, p67SRF and p62TCF (previously called p62), are required to interact with the SRE for efficient induction of c-fos by serum. By quantitative band shift electrophoresis we measure at least a 50-fold increase in SRE affinity for p67SRF/p62TCF over p67SRF alone. Stoichiometrically we determine that the ternary complex with p62TCF involves p67SRF in dimeric form. We demonstrate that p67SRF is a glycosylated nuclear transcription factor carrying terminal N-acetylglucosamine (GlcNAc) as a post-translational modification. A proteolytic limit digestion product, approximately 13 kd in size, was generated from the p67SRF-SRE complex. This p67SRF-core domain binds SRE, can dimerize with p67SRF and is still able to form a ternary complex with p62TCF. Therefore, three functional activities can be ascribed to this small p67SRF-core domain: specific DNA binding, dimerization and interaction with p62TCF. We demonstrate that these functions map within the p67SRF core fragment containing the region between amino acids 93 and 222.},
keywords = {Base Sequence, Chloroquine, Gene Expression Regulation, Genetic, Glycosylation, HeLa Cells, Humans, Kinetics, Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Oligonucleotide Probes, Plasmids, Polymerase Chain Reaction, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Serum Response Factor, Team-Mueller, Transcription, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}