• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

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

转录终止因子rho是一种RNA-DNA解旋酶。

Transcription termination factor rho is an RNA-DNA helicase.

作者信息

Brennan C A, Dombroski A J, Platt T

出版信息

Cell. 1987 Mar 27;48(6):945-52. doi: 10.1016/0092-8674(87)90703-3.

DOI:10.1016/0092-8674(87)90703-3
PMID:3030561
Abstract

E. coli rho factor can unwind a short RNA-DNA duplex in vitro. The duplex is formed between a polylinker sequence at the 3' end of RNA derived from the rho-dependent terminator trp t' and the complementary sequence in a single-strand DNA molecule. Release of trp t' RNA from the duplex requires nucleoside triphosphate hydrolysis by rho's NTPase activity and is dependent on rho recognition of the RNA that is 5' to the RNA-DNA duplex region. The direction of helix unwinding appears to be 5' to 3' along the RNA molecule. These characteristics now account for how the RNA-binding and RNA-dependent NTP hydrolysis activities of rho may participate directly in transcription termination. Our results suggest that NTP hydrolysis is utilized to help unwind the RNA-DNA duplex at the 3' end of a nascent transcript, facilitating RNA release from the DNA template.

摘要

大肠杆菌rho因子在体外可解开一段短的RNA-DNA双链体。该双链体是由源自rho依赖性终止子trp t'的RNA 3'端的多克隆位点序列与单链DNA分子中的互补序列形成的。从双链体中释放trp t' RNA需要rho的NTPase活性水解核苷三磷酸,并且依赖于rho对RNA-DNA双链体区域5'端RNA的识别。螺旋解旋方向似乎是沿着RNA分子从5'到3'。这些特性现在解释了rho的RNA结合和RNA依赖性NTP水解活性如何可能直接参与转录终止。我们的结果表明,利用NTP水解来帮助解开新生转录本3'端的RNA-DNA双链体,促进RNA从DNA模板上释放。

相似文献

1
Transcription termination factor rho is an RNA-DNA helicase.转录终止因子rho是一种RNA-DNA解旋酶。
Cell. 1987 Mar 27;48(6):945-52. doi: 10.1016/0092-8674(87)90703-3.
2
Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 2. Processivity, ATP consumption, and RNA binding.大肠杆菌转录终止因子rho的RNA-DNA解旋酶活性动力学。2. 持续合成能力、ATP消耗及RNA结合
Biochemistry. 1997 Jul 1;36(26):7993-8004. doi: 10.1021/bi963180r.
3
Rho-dependent termination and concomitant NTPase activity requires a specific, intact RNA region.ρ因子依赖性终止及相伴的NTP酶活性需要一个特定的、完整的RNA区域。
J Biol Chem. 1984 Feb 25;259(4):2268-73.
4
Kinetics of the RNA-DNA helicase activity of Escherichia coli transcription termination factor rho. 1. Characterization and analysis of the reaction.大肠杆菌转录终止因子rho的RNA-DNA解旋酶活性动力学。1. 反应的表征与分析。
Biochemistry. 1997 Jul 1;36(26):7980-92. doi: 10.1021/bi963179s.
5
Evidence supporting a tethered tracking model for helicase activity of Escherichia coli Rho factor.支持大肠杆菌Rho因子解旋酶活性的束缚追踪模型的证据。
Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1401-5. doi: 10.1073/pnas.91.4.1401.
6
Influence of substrate composition on the helicase activity of transcription termination factor Rho: reduced processivity of Rho hexamers during unwinding of RNA-DNA hybrid regions.底物组成对转录终止因子Rho解旋酶活性的影响:Rho六聚体在RNA-DNA杂交区域解旋过程中的持续合成能力降低。
J Mol Biol. 2004 Sep 10;342(2):403-20. doi: 10.1016/j.jmb.2004.07.026.
7
Rho-dependent termination within the trp t' terminator. I. Effects of rho loading and template sequence.色氨酸t'终止子内的ρ因子依赖性终止。I. ρ因子加载和模板序列的影响。
Biochemistry. 1998 Aug 11;37(32):11202-14. doi: 10.1021/bi9729110.
8
Specificity and efficiency of rho-factor helicase activity depends on magnesium concentration and energy coupling to NTP hydrolysis.rho因子解旋酶活性的特异性和效率取决于镁离子浓度以及与NTP水解的能量偶联。
J Biol Chem. 1990 Apr 5;265(10):5440-7.
9
Transcription factor Rho does not require a free end to act as an RNA-DNA helicase on an RNA.转录因子Rho在RNA上作为RNA-DNA解旋酶发挥作用时不需要游离末端。
J Biol Chem. 2001 May 18;276(20):17106-10. doi: 10.1074/jbc.M101856200. Epub 2001 Mar 6.
10
Simple enzymatic assays for the in vitro motor activity of transcription termination factor Rho from Escherichia coli.用于检测大肠杆菌转录终止因子Rho体外运动活性的简单酶促测定法。
Methods Mol Biol. 2010;587:137-54. doi: 10.1007/978-1-60327-355-8_10.

引用本文的文献

1
Recent advances in mycobacterial transcription: insights beyond the general pathway.分枝杆菌转录的最新进展:超越一般途径的见解
J Bacteriol. 2025 Jul 24;207(7):e0015425. doi: 10.1128/jb.00154-25. Epub 2025 Jun 24.
2
Rho-dependent transcription termination: mechanisms and roles in bacterial fitness and adaptation to environmental changes.Rho 依赖性转录终止:细菌适应性及对环境变化响应中的机制与作用
RNA. 2025 Aug 18;31(9):1207-1234. doi: 10.1261/rna.080486.125.
3
The bacterial transcription terminator, Rho, functions as an RNA:DNA hybrid (RDH) helicase in vivo.
细菌转录终止因子Rho在体内作为一种RNA:DNA杂交体(RDH)解旋酶发挥作用。
Biochem J. 2025 May 26;482(11):BCJ20253089. doi: 10.1042/BCJ20253089.
4
A widely conserved protein Rof inhibits transcription termination factor Rho and promotes Salmonella virulence program.一种广泛保守的蛋白 Rof 抑制转录终止因子 Rho 并促进沙门氏菌毒力程序。
Nat Commun. 2024 Apr 15;15(1):3187. doi: 10.1038/s41467-024-47438-7.
5
A trailing ribosome speeds up RNA polymerase at the expense of transcript fidelity via force and allostery.尾随核糖体通过力和变构作用提高 RNA 聚合酶的速度,但其代价是转录保真度。
Cell. 2023 Mar 16;186(6):1244-1262.e34. doi: 10.1016/j.cell.2023.02.008.
6
Structural basis of the transcription termination factor Rho engagement with transcribing RNA polymerase from .转录终止因子 Rho 与正在转录的 RNA 聚合酶结合的结构基础。
Sci Adv. 2023 Feb 10;9(6):eade7093. doi: 10.1126/sciadv.ade7093. Epub 2023 Feb 8.
7
Structural basis of Rho-dependent transcription termination.Rho 依赖型转录终止的结构基础。
Nature. 2023 Feb;614(7947):367-374. doi: 10.1038/s41586-022-05658-1. Epub 2023 Jan 25.
8
Protein structure terminates doubt about how transcription stops.蛋白质结构消除了关于转录如何终止的疑问。
Nature. 2023 Feb;614(7947):237-238. doi: 10.1038/d41586-023-00121-1.
9
Two Distinct Modes of DNA Binding by an MCM Helicase Enable DNA Translocation.两种不同的 DNA 结合模式使 MCM 解旋酶能够进行 DNA 易位。
Int J Mol Sci. 2022 Nov 24;23(23):14678. doi: 10.3390/ijms232314678.
10
Factor-stimulated intrinsic termination: getting by with a little help from some friends.因子刺激的内在终止:借助朋友的一点帮助完成任务。
Transcription. 2022 Aug-Oct;13(4-5):96-108. doi: 10.1080/21541264.2022.2127602. Epub 2022 Sep 25.