题名 | Crystal structure of the BRPF2 PWWP domain in complex with DNA reveals a different binding mode than the HDGF family of PWWP domains |
作者 | |
通讯作者 | Min,Jinrong |
发表日期 | 2021-03-01
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DOI | |
发表期刊 | |
ISSN | 1874-9399
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EISSN | 1876-4320
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卷号 | 1864期号:3 |
摘要 | The PWWP domain was first identified in the HDGF protein family and named after the conserved Proline-Tryptophan-Tryptophan-Proline motif in WHSC1. The PWWP domain-containing proteins play important roles in different biological processes, such as DNA replication, transcription, DNA repair, pre-mRNA processing by recognizing methylated histone and dsDNA simultaneously. Recently, how the HDGF family of PWWP domains recognize histone H3K36me3-modified nucleosome has been reported. In order to better understand the interactions between the PWWP domain and dsDNA, we carried out family-wide characterization of dsDNA binding abilities of human PWWP domains. Our binding assays confirmed that PWWP domains bind to dsDNA without sequence selectivity. Our crystal structure of the BRPF2 PWWP domain in complex with a 12-mer dsDNA reveals that the PWWP domain interacts with dsDNA by binding to its major groove, instead of the minor groove observed in the HDGF family of PWWP domains. Our study indicates that PWWP domains could bind to dsDNA in different modes. |
关键词 | |
相关链接 | [Scopus记录] |
收录类别 | |
语种 | 英语
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学校署名 | 其他
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WOS记录号 | WOS:000641019800004
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Scopus记录号 | 2-s2.0-85100727972
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来源库 | Scopus
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引用统计 |
被引频次[WOS]:13
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成果类型 | 期刊论文 |
条目标识符 | http://sustech.caswiz.com/handle/2SGJ60CL/221603 |
专题 | 南方科技大学 生命科学学院 |
作者单位 | 1.College of Pharmaceutical Sciences,Soochow University,Suzhou,China 2.Hubei Key Laboratory of Genetic Regulation and Integrative Biology,School of Life Sciences,Central China Normal University,Wuhan,China 3.Life Science Research Center,Southern University of Science and Technology,Shenzhen,China 4.Structural Genomics Consortium,University of Toronto,Toronto,Canada 5.Donnelly Centre for Cellular and Biomolecular Research,University of Toronto,Toronto,Canada 6.Department of Physiology,University of Toronto,Toronto,Canada |
推荐引用方式 GB/T 7714 |
Zhang,Mengmeng,Lei,Ming,Qin,Su,et al. Crystal structure of the BRPF2 PWWP domain in complex with DNA reveals a different binding mode than the HDGF family of PWWP domains[J]. Biochimica et Biophysica Acta-Gene Regulatory Mechanisms,2021,1864(3).
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APA |
Zhang,Mengmeng.,Lei,Ming.,Qin,Su.,Dong,Aiping.,Yang,Ally.,...&Liu,Yanli.(2021).Crystal structure of the BRPF2 PWWP domain in complex with DNA reveals a different binding mode than the HDGF family of PWWP domains.Biochimica et Biophysica Acta-Gene Regulatory Mechanisms,1864(3).
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MLA |
Zhang,Mengmeng,et al."Crystal structure of the BRPF2 PWWP domain in complex with DNA reveals a different binding mode than the HDGF family of PWWP domains".Biochimica et Biophysica Acta-Gene Regulatory Mechanisms 1864.3(2021).
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