دورية أكاديمية
أعرض في EDS

CMG helicase disassembly is controlled by replication fork DNA, replisome components and a ubiquitin threshold.

التفاصيل البيبلوغرافية
العنوان: CMG helicase disassembly is controlled by replication fork DNA, replisome components and a ubiquitin threshold.
المؤلفون: Deegan TD; The MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, United Kingdom., Mukherjee PP; The MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, United Kingdom., Fujisawa R; The MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, United Kingdom., Polo Rivera C; The MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, United Kingdom., Labib K; The MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, United Kingdom.
المصدر: ELife [Elife] 2020 Aug 17; Vol. 9. Date of Electronic Publication: 2020 Aug 17.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: DNA*/chemistry , DNA*/metabolism , DNA Helicases*/chemistry , DNA Helicases*/metabolism , DNA Replication* , Ubiquitin*/chemistry , Ubiquitin*/metabolism, Escherichia coli ; Humans ; Nucleic Acid Conformation ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Valosin Containing Protein/chemistry ; Valosin Containing Protein/metabolism
مستخلص: The eukaryotic replisome assembles around the CMG helicase, which stably associates with DNA replication forks throughout elongation. When replication terminates, CMG is ubiquitylated on its Mcm7 subunit and disassembled by the Cdc48/p97 ATPase. Until now, the regulation that restricts CMG ubiquitylation to termination was unknown, as was the mechanism of disassembly. By reconstituting these processes with purified budding yeast proteins, we show that ubiquitylation is tightly repressed throughout elongation by the Y-shaped DNA structure of replication forks. Termination removes the repressive DNA structure, whereupon long K48-linked ubiquitin chains are conjugated to CMG-Mcm7, dependent on multiple replisome components that bind to the ubiquitin ligase SCF Dia2 . This mechanism pushes CMG beyond a '5-ubiquitin threshold' that is inherent to Cdc48, which specifically unfolds ubiquitylated Mcm7 and thereby disassembles CMG. These findings explain the exquisite regulation of CMG disassembly and provide a general model for the disassembly of ubiquitylated protein complexes by Cdc48.
Competing Interests: TD, PM, RF, CP, KL No competing interests declared
(© 2020, Deegan et al.)
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معلومات مُعتمدة: 24558 United Kingdom CRUK_ Cancer Research UK; MC_UU_12016/13 United Kingdom MRC_ Medical Research Council; C578/A25669 United Kingdom CRUK_ Cancer Research UK; United Kingdom WT_ Wellcome Trust; C578/A24558 United Kingdom CRUK_ Cancer Research UK; MC_UU_00018/4 United Kingdom MRC_ Medical Research Council
فهرسة مساهمة: Keywords: CMG helicase; DNA replication; S. cerevisiae; chromosomes; gene expression; termination
المشرفين على المادة: 0 (Recombinant Proteins)
0 (Ubiquitin)
9007-49-2 (DNA)
EC 3.6.4.- (DNA Helicases)
EC 3.6.4.6 (Valosin Containing Protein)
تواريخ الأحداث: Date Created: 20200818 Date Completed: 20210225 Latest Revision: 20240313
رمز التحديث: 20240313
مُعرف محوري في PubMed: PMC7462611
DOI: 10.7554/eLife.60371
PMID: 32804080
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.60371