Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Régine Barbey"'
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2010, 38 (15), pp.4998-5014. ⟨10.1093/nar/gkq257⟩
Nucleic Acids Research, 2010, 38 (15), pp.4998-5014. ⟨10.1093/nar/gkq257⟩
Nucleic Acids Research, Oxford University Press, 2010, 38 (15), pp.4998-5014. ⟨10.1093/nar/gkq257⟩
Nucleic Acids Research, 2010, 38 (15), pp.4998-5014. ⟨10.1093/nar/gkq257⟩
International audience; Cell adaptation to the environment often involves induction of complex gene expression programs under the control of specific transcriptional activators. For instance, in response to cadmium, budding yeast induces transcriptio
Publikováno v:
Molecular Cell. 10:69-80
The ubiquitin system has been recently implicated in various aspects of transcriptional regulation, including proteasome-dependent degradation of transcriptional activators. In yeast, the activator Met4 is inhibited by the SCF Met30 ubiquitin ligase,
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2013, 41 (21), pp.9651-9662. ⟨10.1093/nar/gkt701⟩
Nucleic Acids Research, 2013, 41 (21), pp.9651-9662. ⟨10.1093/nar/gkt701⟩
Nucleic Acids Research, Oxford University Press, 2013, 41 (21), pp.9651-9662. ⟨10.1093/nar/gkt701⟩
Nucleic Acids Research, 2013, 41 (21), pp.9651-9662. ⟨10.1093/nar/gkt701⟩
International audience; Mediator is a prominent multisubunit coactivator that functions as a bridge between gene-specific activators and the basal RNA polymerase (Pol) II initiation machinery. Here, we study the poorly documented role of Mediator in
Publikováno v:
FEBS Letters. 323:289-293
The Saccharomyces cerevisiae HOM6 gene, encoding homoserine dehydrogenase (EC 1.1.1.3) was cloned and its nucleotide sequence determined. The yeast homoserine dehydrogenase shows extensive homology to the homoserine dehydrogenase domains of the two a
Publikováno v:
Journal of Biological Chemistry. 265:15518-15524
In yeast, mutations in six different loci (MET1, MET4, MET8, MET16, MET22, and MET25) have been reported to result in the absence of 3'-phosphoadenylylsulfate (PAPS) reductase activity. In the present study, we show that MET16 is the structural gene
Publikováno v:
EMBO Journal
EMBO Journal, EMBO Press, 2006, 25 (19), pp.4436-47. ⟨10.1038/sj.emboj.7601330⟩
EMBO Journal, EMBO Press, 2006, 25 (19), pp.4436-47. ⟨10.1038/sj.emboj.7601330⟩
Plasma membrane transport of single amino-acid methionine in yeast is shown to be mediated by at least seven different permeases whose activities are transcriptionaly and post-transcriptionaly regulated by different ubiquitin-dependent mechanisms. Up
Autor:
Peggy Baudouin-Cornu, Dominique Thomas, Patrick Zarzov, Astrid Rouillon, Traci A Lee, Régine Barbey, Mike Tyers
Publikováno v:
The EMBO journal. 24(3)
Activity of the Met4 transcription factor is antagonized by the SCF(Met30) ubiquitin ligase by degradation-dependent and degradation-independent mechanisms, in minimal and rich nutrient conditions, respectively. In this study, we show that the heavy
Publikováno v:
The EMBO journal. 19(2)
Saccharomyces cerevisiae SCF(Met30) ubiquitin-protein ligase controls cell cycle function and sulfur amino acid metabolism. We report here that the SCF(Met30 )complex mediates the transcriptional repression of the MET gene network by triggering degra
Autor:
Régine Barbey, Jean-Pierre Cartron, Valérie Camara-Clayette, Cécile Rahuel, Olivier F. Bertrand, Dominique Thomas
Glycophorin B (GPB) is an abundant cell surface glycoprotein which is only expressed in human erythroid cells. Previous functional analysis demonstrated that the repression of the GPB promoter is determined by the binding of a ubiquitous factor which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::441cd2992eef32cfb1c934ac2f284f25
https://europepmc.org/articles/PMC148369/
https://europepmc.org/articles/PMC148369/
Publikováno v:
The EMBO journal. 16(9)
Transcriptional activation of sulfur amino acid metabolism in yeast is dependent on a multi‐functional factor, the centromere‐binding factor 1 (Cbf1) and on two specific transcription factors, Met4 and Met28. Cbf1 belongs to the basic helix–loo