气候变化领域集成服务门户(CCPortal): Cockayne syndrome B protein acts as an ATP-dependent processivity factor that helps RNA polymerase II overcome nucleosome barriers

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DOI	10.1073/pnas.2013379117
	Cockayne syndrome B protein acts as an ATP-dependent processivity factor that helps RNA polymerase II overcome nucleosome barriers
	Xu J.; Wang W.; Xu L.; Chen J.-Y.; Chong J.; Oh J.; Leschziner A.E.; Fu X.-D.; Wang D.
发表日期	2020
ISSN	0027-8424
起始页码	25486
结束页码	25493
卷号	117 期号:41
英文摘要	While loss-of-function mutations in Cockayne syndrome group B protein (CSB) cause neurological diseases, this unique member of the SWI2/SNF2 family of chromatin remodelers has been broadly implicated in transcription elongation and transcription-coupled DNA damage repair, yet its mechanism remains largely elusive. Here, we use a reconstituted in vitro transcription system with purified polymerase II (Pol II) and Rad26, a yeast ortholog of CSB, to study the role of CSB in transcription elongation through nucleosome barriers. We show that CSB forms a stable complex with Pol II and acts as an ATP-dependent processivity factor that helps Pol II across a nucleosome barrier. This noncanonical mechanism is distinct from the canonical modes of chromatin remodelers that directly engage and remodel nucleosomes or transcription elongation factors that facilitate Pol II nucleosome bypass without hydrolyzing ATP. We propose a model where CSB facilitates gene expression by helping Pol II bypass chromatin obstacles while maintaining their structures. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	Chromatin remodeling; Cockayne syndrome; Nucleosome bypass; RNA polymerase II; Transcription elongation
语种	英语
scopus关键词	adenosine triphosphatase; cell membrane protein; Cockayne syndrome group B protein; nucleic acid binding protein; Rad26 protein; RNA polymerase II; unclassified drug; adenosine triphosphatase; adenosine triphosphate; DNA helicase; DNA ligase; ERCC6 protein, human; fungal DNA; poly ADP ribose binding protein; RAD26 protein, S cerevisiae; RNA polymerase II; Saccharomyces cerevisiae protein; Article; binding affinity; cell membrane permeability; chromatin assembly and disassembly; chromatin immunoprecipitation sequencing; chromatin structure; controlled study; DNA repair; Escherichia coli; gene expression; in vitro study; nonhuman; nucleosome; priority journal; protein analysis; protein function; protein localization; protein structure; Saccharomyces cerevisiae; transcription elongation; transcription regulation; gene expression regulation; genetics; metabolism; molecular model; mutation; protein conformation; Schizosaccharomyces; Adenosine Triphosphatases; Adenosine Triphosphate; DNA Helicases; DNA Repair Enzymes; DNA, Fungal; Escherichia coli; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Fungal; Models, Molecular; Mutation; Nucleosomes; Poly-ADP-Ribose Binding Proteins; Protein Conformation; RNA Polymerase II; Saccharomyces cerevisiae Proteins; Schizosaccharomyces
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160210
作者单位	Xu, J., Division of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, San diego, CA 92093, United States; Wang, W., Division of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, San diego, CA 92093, United States; Xu, L., Division of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, San diego, CA 92093, United States; Chen, J.-Y., Department of Cellular and Molecular Medicine, University of California San Diego, San diego, CA 92093, United States; Chong, J., Division of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, San diego, CA 92093, United States; Oh, J., Division of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, San diego, CA 92093, United States; Leschziner, A.E.,...
推荐引用方式 GB/T 7714	Xu J.,Wang W.,Xu L.,et al. Cockayne syndrome B protein acts as an ATP-dependent processivity factor that helps RNA polymerase II overcome nucleosome barriers[J],2020,117(41).
APA	Xu J..,Wang W..,Xu L..,Chen J.-Y..,Chong J..,...&Wang D..(2020).Cockayne syndrome B protein acts as an ATP-dependent processivity factor that helps RNA polymerase II overcome nucleosome barriers.Proceedings of the National Academy of Sciences of the United States of America,117(41).
MLA	Xu J.,et al."Cockayne syndrome B protein acts as an ATP-dependent processivity factor that helps RNA polymerase II overcome nucleosome barriers".Proceedings of the National Academy of Sciences of the United States of America 117.41(2020).