ArticleJournal of bacteriology2006
Cysteine-scanning analysis of the chemoreceptor-coupling domain of the Escherichia coli chemotaxis signaling kinase CheA.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Protein-protein interfaces in chemotaxis receptor complexes and their role in signaling.FEMS microbiology reviews · 2026Review
- Structural signatures ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Regulation of the chemotaxis histidine kinase CheA: A structural perspective.Biochimica et biophysica acta. Biomembranes · 2020Review
- Noncritical Signaling Role of a Kinase-Receptor Interaction Surface in the Escherichia coli Chemosensory Core Complex.Journal of molecular biology · 2018Article
- Chemotaxis arrays inJournal of bacteriology · 2018Article
- Article
- The source of high signal cooperativity in bacterial chemosensory arrays.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update.Trends in microbiology · 2015Review
- Signalling-dependent interactions between the kinase-coupling protein CheW and chemoreceptors in living cells.Molecular microbiology · 2014Article
- Article
- Mutational analysis of the P1 phosphorylation domain in Escherichia coli CheA, the signaling kinase for chemotaxis.Journal of bacteriology · 2014Article
- Article
- The mobility of two kinase domains in the Escherichia coli chemoreceptor array varies with signalling state.Molecular microbiology · 2013Article
- Article
- Computational and experimental analyses reveal the essential roles of interdomain linkers in the biological function of chemotaxis histidine kinase CheA.Journal of the American Chemical Society · 2012Article
- Molecular architecture of chemoreceptor arrays revealed by cryoelectron tomography of Escherichia coli minicells.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Protein footprinting in a complex milieu: identifying the interaction surfaces of the chemotaxis adaptor protein CheW.Journal of molecular biology · 2011Article
- Structural biology by mass spectrometry: mapping protein interaction surfaces of membrane receptor complexes with ICAT.Journal of molecular biology · 2011Article
- Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The C-terminal P5 domain of the histidine kinase CheA is essential for coupling CheA autophosphorylation activity to chemoreceptor control through a binding interaction with the CheW protein. To locate P5 determinants critical for CheW binding and chemoreceptor control, we surveyed cysteine replacements at 39 residues predicted to be at or near the P5 surface in Escherichia coli CheA. Two-thirds of the Cys replacement proteins exhibited in vitro defects in CheW binding, either before or after modification with a bulky fluorescein group. The binding-defective sites were widely distributed on the P5 surface and were often interspersed with sites that caused no functional defects, implying that relatively minor structural perturbations, often far from the actual binding site, can influence its conformation or accessibility. The most likely CheW docking area included loop 2 in P5 folding subdomain 1. All but four of the binding-defective P5-Cys proteins were defective in receptor-mediated activation, suggesting that CheW binding, as measured in vitro, is necessary for assembly of ternary signaling complexes and/or subsequent CheA activation. Other Cys sites specifically affected receptor-mediated activation or deactivation of CheA, demonstrating that CheW binding is not sufficient for assembly and/or operation of receptor signaling complexes. Because P5 is quite similar to CheW, whose structure is known to be dynamic, we suggest that conformational flexibility and dynamic motions govern the signaling activities of the P5 domain. In addition, relative movements of the CheA domains may be involved in CheW binding, in ternary complex assembly, and in subsequent stimulus-induced conformational changes in receptor signaling complexes.
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