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  • 标题:Proton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coli translocase.
  • 本地全文:下载
  • 作者:A J Driessen ; W Wickner
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1991
  • 卷号:88
  • 期号:6
  • 页码:2471-2475
  • DOI:10.1073/pnas.88.6.2471
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:The protonmotive force stimulates translocation in vivo, in crude in vitro reactions, and in a purified, reconstituted reaction. Translocation activity is a function of the pH at the inner face of the membrane. Both the transmembrane pH gradient and the transmembrane electrical potential stimulate translocation. A late-stage translocation intermediate of the proOmpA preprotein completes its translocation in the absence of ATP when a protonmotive force is imposed. This completion of translocation is retarded by a factor of greater than 3 in deuterium oxide relative to water, demonstrating that translocation involves proton-transfer reactions in rate-limiting steps.
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