气候变化领域集成服务门户(CCPortal): Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination

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DOI	10.1073/pnas.2025291118
	Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination
	Chen F.; Liu B.; Guo L.; Ge X.; Feng W.; Li D.-F.; Zhou H.; Long J.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:33
英文摘要	The highly conserved multifunctional polymerase-associated factor 1 (Paf1) complex (PAF1C), composed of five core subunits Paf1, Leo1, Ctr9, Cdc73, and Rtf1, participates in all stages of transcription and is required for the Rad6/Bre1-mediated monoubiquitination of histone H2B (H2Bub). However, the molecular mechanisms underlying the contributions of the PAF1C subunits to H2Bub are not fully understood. Here, we report that Ctr9, acting as a hub, interacts with the carboxyl-terminal acidic tail of Rad6, which is required for PAF1C-induced stimulation of H2Bub. Importantly, we found that the Ras-like domain of Cdc73 has the potential to accelerate ubiquitin discharge from Rad6 and thus facilitates H2Bub, a process that might be conserved from yeast to humans. Moreover, we found that Rtf1 HMD stimulates H2Bub, probably through accelerating ubiquitin discharge from Rad6 alone or in cooperation with Cdc73 and Bre1, and that the Paf1/Leo1 heterodimer in PAF1C specifically recognizes the histone H3 tail of nucleosomal substrates, stimulating H2Bub. Collectively, our biochemical results indicate that intact PAF1C is required to efficiently stimulate Rad6/Bre1-mediated H2Bub. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Cooperation; H2B monoubiquitination; Paf1 complex; Rad6/Bre1; Ubiquitin discharge
语种	英语
scopus关键词	DNA polymerase; heterodimer; histone H2B; membrane protein; polymerase associated factor 1 complex; ubiquitin; unclassified drug; Bre1 protein, S cerevisiae; CDC73 protein, S cerevisiae; cell cycle protein; CTR9 protein, S cerevisiae; histone; Leo1 protein, S cerevisiae; nuclear protein; PAF1 protein, S cerevisiae; RAD6 protein, S cerevisiae; RNA binding protein; RTF1 protein, S cerevisiae; Saccharomyces cerevisiae protein; TATA binding protein; transcription elongation factor; ubiquitin conjugating enzyme; Article; binding affinity; biochemistry; carboxy terminal sequence; complex formation; genetic conservation; genetic transcription; in vitro study; monoubiquitination; nonhuman; protein domain; protein expression; protein protein interaction; protein quaternary structure; protein transport; ubiquitination; yeast; Escherichia coli; gene expression regulation; genetics; metabolism; molecular cloning; nucleosome; protein subunit; Saccharomyces cerevisiae; Cell Cycle Proteins; Cloning, Molecular; Escherichia coli; Gene Expression Regulation, Fungal; Histones; Nuclear Proteins; Nucleosomes; Protein Subunits; RNA-Binding Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; TATA-Box Binding Protein; Transcriptional Elongation Factors; Ubiquitin-Conjugating Enzymes
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/251055
作者单位	State Key Laboratory of Medicinal Chemical Biology, Tianjin Key Laboratory of Protein Science, Nankai University, Tianjin, 300071, China; College of Life Sciences, Nankai University, Tianjin, 300071, China; State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China; National Laboratory of Biomacromolecules, Chinese Academy of Sciences Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China; College of Life Sciences, University of Chinese Academy of Sciences, Beijing, 100049, China
推荐引用方式 GB/T 7714	Chen F.,Liu B.,Guo L.,et al. Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination[J],2021,118(33).
APA	Chen F..,Liu B..,Guo L..,Ge X..,Feng W..,...&Long J..(2021).Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination.Proceedings of the National Academy of Sciences of the United States of America,118(33).
MLA	Chen F.,et al."Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination".Proceedings of the National Academy of Sciences of the United States of America 118.33(2021).