• 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

阻碍负载下生物分子马达的非紧密和紧密化学机械耦合

Non-tight and tight chemomechanical couplings of biomolecular motors under hindering loads.

作者信息

Xie Ping

机构信息

Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.

出版信息

J Theor Biol. 2020 Apr 7;490:110173. doi: 10.1016/j.jtbi.2020.110173. Epub 2020 Jan 23.

DOI:10.1016/j.jtbi.2020.110173
PMID:31982418
Abstract

Biomolecular motors make use of free energy released from chemical reaction (typically ATP hydrolysis) to perform mechanical motion or work. An important issue is whether a molecular motor exhibits tight or non-tight chemomechanical (CM) coupling. The tight CM coupling refers to that each ATPase activity is coupled with a mechanical step, while the non-tight CM coupling refers to that an ATPase activity is not necessarily coupled with a mechanical step. Here, we take kinesin, monomeric DNA helicase, ring-shaped hexameric DNA helicase and ribosome as examples to study this issue. Our studies indicate that some motors such as kinesin, monomeric helicase and ribosome exhibit non-tight CM coupling under hindering forces, while others such as the ring-shaped hexameric helicase exhibit tight or nearly tight CM coupling under any force. For the former, the reduction of the velocity caused by the hindering force arises mainly from the reduction of the CM coupling efficiency, while the ATPase rate is independent or nearly independent of the force. For the latter, the reduction of the velocity caused by the hindering force arises mainly from the reduction of the ATPase rate, while the CM coupling efficiency is independent or nearly independent of the force.

摘要

生物分子马达利用化学反应(通常是ATP水解)释放的自由能来执行机械运动或功。一个重要的问题是分子马达是否表现出紧密或非紧密的化学机械(CM)偶联。紧密的CM偶联是指每个ATP酶活性与一个机械步骤偶联,而非紧密的CM偶联是指一个ATP酶活性不一定与一个机械步骤偶联。在这里,我们以驱动蛋白、单体DNA解旋酶、环状六聚体DNA解旋酶和核糖体为例来研究这个问题。我们的研究表明,一些马达,如驱动蛋白、单体解旋酶和核糖体,在阻碍力下表现出非紧密的CM偶联,而其他一些,如环状六聚体解旋酶,在任何力下都表现出紧密或近乎紧密的CM偶联。对于前者,阻碍力导致的速度降低主要源于CM偶联效率的降低,而ATP酶速率与力无关或几乎与力无关。对于后者,阻碍力导致的速度降低主要源于ATP酶速率的降低,而CM偶联效率与力无关或几乎与力无关。

相似文献

1
Non-tight and tight chemomechanical couplings of biomolecular motors under hindering loads.阻碍负载下生物分子马达的非紧密和紧密化学机械耦合
J Theor Biol. 2020 Apr 7;490:110173. doi: 10.1016/j.jtbi.2020.110173. Epub 2020 Jan 23.
2
ATP-Concentration- and Force-Dependent Chemomechanical Coupling of Kinesin Molecular Motors.肌球蛋白分子马达的 ATP 浓度和力依赖性化学机械偶联。
J Chem Inf Model. 2019 Jan 28;59(1):360-372. doi: 10.1021/acs.jcim.8b00577. Epub 2018 Dec 17.
3
A model for the chemomechanical coupling of the mammalian cytoplasmic dynein molecular motor.哺乳动物细胞质动力蛋白分子马达的化学机械耦联模型。
Eur Biophys J. 2019 Oct;48(7):609-619. doi: 10.1007/s00249-019-01386-z. Epub 2019 Jul 5.
4
A Generalized Kinetic Model for Coupling between Stepping and ATP Hydrolysis of Kinesin Molecular Motors.一种用于连接分子马达的步移与 ATP 水解的广义动力学模型。
Int J Mol Sci. 2019 Oct 3;20(19):4911. doi: 10.3390/ijms20194911.
5
A common chemomechanical coupling model for orphan and conventional kinesin molecular motors.一种常见的孤儿和传统驱动蛋白分子马达的化学生物耦合模型。
Biophys Chem. 2020 Sep;264:106427. doi: 10.1016/j.bpc.2020.106427. Epub 2020 Jul 8.
6
A non-tight chemomechanical coupling model for force-dependence of movement dynamics of molecular motors.一种非紧密化学机械耦合模型,用于研究分子马达运动动力学对力的依赖性。
Phys Chem Chem Phys. 2018 Feb 14;20(7):4752-4759. doi: 10.1039/c7cp05557a.
7
Single molecule processes on the stepwise movement of ATP-driven molecular motors.ATP驱动分子马达逐步运动中的单分子过程。
Biosystems. 2003 Sep;71(1-2):145-56. doi: 10.1016/s0303-2647(03)00122-9.
8
On the hand-over-hand mechanism of kinesin.关于驱动蛋白的手换手机制。
Proc Natl Acad Sci U S A. 2006 May 23;103(21):8072-7. doi: 10.1073/pnas.0602828103. Epub 2006 May 12.
9
Generic maps of optimality reveal two chemomechanical coupling regimes for motor proteins: from F-ATPase and kinesin to myosin and cytoplasmic dynein.最优性的通用图谱揭示了驱动蛋白的两种化学机械偶联机制:从F-ATP酶和驱动蛋白到肌球蛋白和胞质动力蛋白。
Integr Biol (Camb). 2018 Jan 22;10(1):34-47. doi: 10.1039/c7ib00142h.
10
Mechanochemical coupling and bi-phasic force-velocity dependence in the ultra-fast ring ATPase SpoIIIE.超快速环 ATP 酶 SpoIIIE 中的机械化学偶联和双相力-速度依赖性。
Elife. 2018 Mar 5;7:e32354. doi: 10.7554/eLife.32354.

引用本文的文献

1
Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.建模驱动蛋白-13 MCAK 和驱动蛋白-14 Cik1-Kar3 分子马达的定向运动。
Protein Sci. 2021 Oct;30(10):2092-2105. doi: 10.1002/pro.4165. Epub 2021 Aug 20.
2
Effect of Kinesin-5 Tail Domain on Motor Dynamics for Antiparallel Microtubule Sliding.驱动蛋白-5 尾部结构域对微管反平行滑动的运动动力学的影响。
Int J Mol Sci. 2021 Jul 23;22(15):7857. doi: 10.3390/ijms22157857.
3
A model of processive walking and slipping of kinesin-8 molecular motors.肌球蛋白-8 分子马达的连续行走和打滑模型。
Sci Rep. 2021 Apr 13;11(1):8081. doi: 10.1038/s41598-021-87532-0.