Publication Type |
pre-print |
School or College |
College of Science |
Department |
Biology |
Creator |
Parkinson, John Stansfield |
Other Author |
Ames, Peter; Zhou, Qin |
Title |
HAMP domain structural determinants for signalling and sensory adaptation in Tsr, the E. coli serine chemoreceptor |
Date |
2014-01-01 |
Description |
Motile Escherichia coli cells track chemical gradients with high sensitivity over wide concentration ranges [recently reviewed in (Hazelbauer et al., 2008; Hazelbauer & Lai, 2010)]. Stimulus detection, amplification, and integration occur in an arrayed network of signaling complexes that contain transmembrane chemoreceptors (methyl-accepting chemotaxis proteins or MCPs), the signaling histidine kinase CheA, and CheW, which couples CheA activity to chemoreceptor control. In the absence of chemoattractant gradients, MCPs activate CheA, promoting frequent episodes of clockwise (CW) flagellar rotation and random changes in swimming direction. Binding of an attractant ligand to the periplasmic sensing domain of a receptor molecule down-regulates CheA bound to the cytoplasmic tip of the receptor (Fig. 1), promoting counter-clockwise (CCW) flagellar rotation and forward swimming. Subsequent sensory adaptation restores pre-stimulus behavior through changes in MCP methylation state, catalyzed by a dedicated methyltransferase (CheR) and methylesterase (CheB). |
Type |
Text |
Publisher |
Wiley-Blackwell |
Volume |
91 |
Issue |
5 |
First Page |
875 |
Last Page |
886 |
Language |
eng |
Bibliographic Citation |
Ames, P., Zhou, Q., & Parkinson, J. S. (2014). HAMP domain structural determinants for signalling and sensory adaptation in Tsr, the Escherichia coli serine chemoreceptor. Molecular Microbiology, 91(5), 875-86. |
Rights Management |
(c) Wiley-Blackwell The definitive version is available at www3.interscience.wiley.com ; This is the pre-peer reviewed version of the following article:Ames, P., Zhou, Q., & Parkinson, J. S. (2014). HAMP domain structural determinants for signalling and sensory adaptation in Tsr, the Escherichia coli serine chemoreceptor. Molecular Microbiology, 91(5), 875-86, which has been published in final form at DOI: 10.1111/mmi.12443 ; http://onlinelibrary.wiley.com/doi/10.1111/mmi.12443/abstract |
Format Medium |
application/pdf |
Format Extent |
2,809,611 bytes |
Identifier |
uspace,18519 |
ARK |
ark:/87278/s6fr35p9 |
Setname |
ir_uspace |
ID |
712280 |
Reference URL |
https://collections.lib.utah.edu/ark:/87278/s6fr35p9 |