期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 105, 期 15, 页码 5891-5896出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0800247105
关键词
replica exchange molecular dynamics simulation; signal transduction; YycG; YycH; Yycl
资金
- NCRR NIH HHS [RR012255, P41 RR012255] Funding Source: Medline
- NIAID NIH HHS [AI055860, R01 AI055860] Funding Source: Medline
- NIGMS NIH HHS [GM019416, R01 GM019416, R37 GM019416, F32 GM019416] Funding Source: Medline
Two-component signal transduction systems with membrane-embedded sensor histidine kinases are believed to recognize environmental signals and transduce this information over the cellular membrane to influence the activity of a transcription factor to which they are mated. The YycG sensor kinase of Bacilius subtilis, containing two transmembrane helices, is subject to a complicated activity-control circuit involving two other proteins with N-terminal transmembrane helices, YycH and Yycl. Truncation studies of YycH and Yycl demonstrated that the individual transmembrane helices of these proteins are sufficient to adjust YycG activity, indicating that this control is achieved at the membrane level. A replica exchange molecular dynamics computational approach generated in silica, structural models of the transmembrane helix complex that informed mutagenesis studies of the Yycl transmembrane helix supporting the accuracy of the in silico model. The results predict that signal recognition by any of the extracellular domains of the sensor histidine kinase YycG or the associated proteins YycH and Yycl is transmitted across the cellular membrane by subtle alterations in the positions of the helices within the transmembrane complex of the three proteins.
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