Suppr超能文献

乳头瘤病毒E1蛋白与人类拓扑异构酶I结合并对其产生刺激作用。

Papillomavirus E1 protein binds to and stimulates human topoisomerase I.

作者信息

Clower Randolph V, Fisk John C, Melendy Thomas

机构信息

Department of Microbiology & Immunology, The School of Medicine and Biomedical Sciences, University at Buffalo, 213 Biomedical Research Building, 3435 Main Street, Buffalo, NY 14214, USA.

出版信息

J Virol. 2006 Feb;80(3):1584-7. doi: 10.1128/JVI.80.3.1584-1587.2006.

Abstract

The papillomavirus (PV) E1 helicase plays a direct role in recruiting cellular DNA replication factors, such as replication protein A or polymerase alpha-primase, to replicate PV genomes. Here, E1 is shown to bind to human topoisomerase I and stimulate its relaxation activity up to sevenfold. The interaction between E1 and topoisomerase I was mapped to the E1 DNA binding domain and C terminus. These findings imply a mechanism for the recruitment of topoisomerase I to PV DNA replication forks and for stimulating topoisomerase I to allow for efficient relaxation of the torsional stress induced by replication fork progression.

摘要

乳头瘤病毒(PV)E1解旋酶在募集细胞DNA复制因子(如复制蛋白A或聚合酶α-引发酶)以复制PV基因组方面发挥直接作用。在此,研究表明E1可与人拓扑异构酶I结合,并将其松弛活性提高多达七倍。E1与拓扑异构酶I之间的相互作用定位于E1 DNA结合结构域和C末端。这些发现揭示了一种机制,可将拓扑异构酶I募集到PV DNA复制叉,并刺激拓扑异构酶I,以便有效缓解复制叉前进所诱导的扭转应力。

相似文献

引用本文的文献

本文引用的文献

6
DNA topoisomerases: structure, function, and mechanism.DNA拓扑异构酶:结构、功能及作用机制
Annu Rev Biochem. 2001;70:369-413. doi: 10.1146/annurev.biochem.70.1.369.
7
Assaying DNA topoisomerase I relaxation activity.
Methods Mol Biol. 2001;95:1-11. doi: 10.1385/1-59259-057-8:1.

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验