دورية أكاديمية

Determinants of the ubiquitin-mediated degradation of the Met4 transcription factor.

التفاصيل البيبلوغرافية
العنوان: Determinants of the ubiquitin-mediated degradation of the Met4 transcription factor.
المؤلفون: Menant, Alexandra, Baudouin-Cornu, Peggy, Peyraud, Caroline, Tyers, Mike, Thomas, Dominique
المساهمون: Centre de génétique moléculaire (CGM), Centre National de la Recherche Scientifique (CNRS), Mount Sinai Hospital Toronto, Canada (MSH), Service de Biochimie et Génétique Moléculaire, CEA/Saclay, Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Génétique et biochimie des microorganismes (GBM), Institut Pasteur Paris (IP)-Centre National de la Recherche Scientifique (CNRS), Cytomics Systems SA, Gif-sur-Yvette, Cytomics Systems SA, CNRS, Association de la Recherche sur le Cancer (ARC) (to D. T.), grants from the National Cancer Institute of Canada and the Canadian Institutes of Health Research (CIHR) (to M. T.). MT supported by a Canada Research Chair in Functional Genomics and Bioinformatics
المصدر: ISSN: 0021-9258.
بيانات النشر: HAL CCSD
American Society for Biochemistry and Molecular Biology
سنة النشر: 2006
المجموعة: HAL-CEA (Commissariat à l'énergie atomique et aux énergies alternatives)
مصطلحات موضوعية: MESH: Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, MESH: Basic-Leucine Zipper Transcription Factors, MESH: Repressor Proteins, MESH: S-Adenosylmethionine, MESH: Saccharomyces cerevisiae, MESH: Saccharomyces cerevisiae Proteins, MESH: Sulfur, MESH: Transcription, Genetic, MESH: Ubiquitin, MESH: Ubiquitin-Protein Ligase Complexes, MESH: Cell Nucleus, MESH: Chromosomal Instability, MESH: Cysteine, MESH: Gene Expression Regulation, Fungal, MESH: Kinetochores, MESH: Methionine, MESH: Proteasome Endopeptidase Complex, MESH: Recombinant Fusion Proteins, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]
الوصف: In yeast, the Met4 transcription factor and its cofactors Cbf1, Met28, Met31, and Met32 control the expression of sulfur metabolism and oxidative stress response genes. Met4 activity is tuned to nutrient and oxidative stress conditions by the SCF(Met30) ubiquitin ligase. The mechanism whereby SCF(Met30)-dependent ubiquitylation of Met4 controls Met4 activity remains contentious. Here, we have demonstrated that intracellular cysteine levels dictate the degradation of Met4 in vivo, as shown by the ability of cysteine, but not methionine or S-adenosylmethionine (AdoMet), to trigger Met4 degradation in an str4Delta strain, which lacks the ability to produce cysteine from methionine or AdoMet. Met4 degradation requires its nuclear localization and activity of the 26 S proteasome. Analysis of the regulated degradation of a fully functional Met4-Cbf1 chimera, in which Met4 is fused to the DNA binding domain of Cbf1, demonstrates that elimination of Met4 in vivo can be triggered independently of both its normal protein interactions. Strains that harbor the Met4-Cbf1 fusion as the only source of Cbf1 activity needed for proper kinetochore function exhibit high rates of methionine-dependent chromosomal instability. We suggest that SCF(Met30) activity or Met4 utilization as a substrate may be directly regulated by intracellular cysteine concentrations.
نوع الوثيقة: article in journal/newspaper
اللغة: English
العلاقة: info:eu-repo/semantics/altIdentifier/pmid/16497670; hal-00132777; https://hal.science/hal-00132777Test; PUBMED: 16497670
DOI: 10.1074/jbc.M600037200
الإتاحة: https://doi.org/10.1074/jbc.M600037200Test
https://hal.science/hal-00132777Test
رقم الانضمام: edsbas.194D4CEE
قاعدة البيانات: BASE