• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >J-Domain Proteins in Bacteria and Their Viruses
【24h】

J-Domain Proteins in Bacteria and Their Viruses

机译：细菌中的J-域蛋白及其病毒

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Molecular chaperones maintain cellular protein homeostasis by acting at almost every step in protein biogenesis pathways. The DnaK/HSP70 chaperone has been associated with almost every known essential chaperone functions in bacteria. To act as a bona fide chaperone, DnaK strictly relies on essential cochaperone partners known as the J-domain proteins (JDPs, DnaJ, Hsp40), which preselect substrate proteins for DnaK, confer its specific cellular localization, and stimulate both its weak ATPase activity and substrate transfer. Remarkably, genome sequencing has revealed the presence of multiple JDP/DnaK chaperone/co-chaperone pairs in a number of bacterial genomes, suggesting that certain pairs have evolved toward more specific functions. In this review, we have used representative sets of bacterial and phage genomes to explore the distribution of JDP/DnaK pairs. Such analysis has revealed an unexpected reservoir of novel bacterial JDPs co-chaperones with very diverse and unexplored function that will be discussed. (C) 2020 Elsevier Ltd. All rights reserved.
机译：分子伴侣通过在蛋白质生物发生途径的几乎每一步中作用来维持细胞蛋白质稳态。 DNAK / HSP70伴侣网已经与细菌中几乎所有已知的必需伴侣功能相关联。为了充当BOA FIDE伴侣，DNAK严格依赖于称为J-域蛋白（JDPS，DNAJ，HSP40）的基本科切蛋白合作伙伴，其预先选择DNAK的底物蛋白，赋予其特定的细胞定位，并刺激其弱ATP酶活性和基材转移。值得注意的是，基因组测序揭示了许多细菌基因组中的多个JDP / DNAK伴侣/共伴侣对的存在，这表明某些对已经发展朝向更具体的功能。在本综述中，我们使用了代表性的细菌和噬菌体基因组探索了JDP / DNAK对的分布。这种分析揭示了一种具有非常多样化和未开发的功能的新型细菌JDPS共伴侣的意外储层。 （c）2020 elestvier有限公司保留所有权利。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号