دورية أكاديمية

The FACT complex interacts with the E3 ubiquitin ligase Psh1 to prevent ectopic localization of CENP-A.

التفاصيل البيبلوغرافية
العنوان: The FACT complex interacts with the E3 ubiquitin ligase Psh1 to prevent ectopic localization of CENP-A.
المؤلفون: Deyter GM; Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA., Biggins S; Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA sbiggins@fhcrc.org.
المصدر: Genes & development [Genes Dev] 2014 Aug 15; Vol. 28 (16), pp. 1815-26.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Cold Spring Harbor Laboratory Press Country of Publication: United States NLM ID: 8711660 Publication Model: Print Cited Medium: Internet ISSN: 1549-5477 (Electronic) Linking ISSN: 08909369 NLM ISO Abbreviation: Genes Dev Subsets: MEDLINE
أسماء مطبوعة: Publication: Cold Spring Harbor, NY : Cold Spring Harbor Laboratory Press
Original Publication: [Cold Spring Harbor, N.Y.] : Cold Spring Harbor Laboratory in association with the Genetical Society of Great Britain, [c1987-
مواضيع طبية MeSH: Autoantigens/*metabolism , Chromosomal Proteins, Non-Histone/*metabolism , DNA-Binding Proteins/*metabolism , High Mobility Group Proteins/*metabolism , Peptide Elongation Factors/*metabolism , Saccharomyces cerevisiae/*physiology , Saccharomyces cerevisiae Proteins/*metabolism , Transcriptional Elongation Factors/*metabolism , Ubiquitin-Protein Ligases/*metabolism, Centromere Protein A ; Euchromatin/metabolism ; Mutation ; Nucleosomes/metabolism ; Peptide Elongation Factors/genetics ; Protein Binding ; Protein Stability ; Protein Transport ; Proteolysis ; Saccharomyces cerevisiae/enzymology ; Ubiquitin-Protein Ligases/genetics ; Ubiquitination
مستخلص: Centromere identity and its epigenetic maintenance require the incorporation of a histone H3 variant called CENP-A at centromeres. CENP-A mislocalization to ectopic sites may disrupt chromatin-based processes and chromosome segregation, so it is important to uncover the mechanisms by which this variant is exclusively localized to centromeres. Here, we identify a role for the conserved chromatin-modifying complex FACT (facilitates chromatin transcription/transactions) in preventing budding yeast CENP-A(Cse4) mislocalization to euchromatin by mediating its proteolysis. The Spt16 subunit of the FACT complex binds to Psh1 (Pob3/Spt16/histone), an E3 ubiquitin ligase that targets CENP-A(Cse4) for degradation. The interaction between Psh1 and Spt16 is critical for both CENP-A(Cse4) ubiquitylation and its exclusion from euchromatin. We found that Psh1 cannot efficiently ubiquitylate CENP-A(Cse4) nucleosomes in vitro, suggesting that additional factors must facilitate CENP-A(Cse4) removal from chromatin in vivo. Consistent with this, a Psh1 mutant that cannot associate with FACT has a reduced interaction with CENP-A(Cse4) in vivo. Together, our data identify a previously unknown mechanism to maintain centromere identity and genomic stability through the FACT-mediated degradation of ectopically localized CENP-A(Cse4).
(© 2014 Deyter and Biggins; Published by Cold Spring Harbor Laboratory Press.)
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معلومات مُعتمدة: P30 CA015704 United States CA NCI NIH HHS; R01 GM078069 United States GM NIGMS NIH HHS; GM078069 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: CENP-A; FACT; Psh1; centromere; proteolysis; ubiquitylation
المشرفين على المادة: 0 (Autoantigens)
0 (Centromere Protein A)
0 (Chromosomal Proteins, Non-Histone)
0 (DNA-Binding Proteins)
0 (Euchromatin)
0 (FACT protein, S cerevisiae)
0 (High Mobility Group Proteins)
0 (Nucleosomes)
0 (Peptide Elongation Factors)
0 (SPT16 protein, S cerevisiae)
0 (Saccharomyces cerevisiae Proteins)
0 (Transcriptional Elongation Factors)
EC 2.3.2.27 (Psh1 protein, S cerevisiae)
EC 2.3.2.27 (Ubiquitin-Protein Ligases)
تواريخ الأحداث: Date Created: 20140817 Date Completed: 20141001 Latest Revision: 20211021
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC4197964
DOI: 10.1101/gad.243113.114
PMID: 25128498
قاعدة البيانات: MEDLINE
الوصف
تدمد:1549-5477
DOI:10.1101/gad.243113.114