ArticleJournal of bacteriology2014
Mutational analysis of the P1 phosphorylation domain in Escherichia coli CheA, the signaling kinase for chemotaxis.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Dynamic domain interactions encode possible CheA autophosphorylation mechanisms revealed by coarse-grained simulations.Biophysical journal · 2026Article
- Dynamic domain interactions encode possible CheA autophosphorylation mechanisms revealed by coarse-grained simulations.bioRxiv : the preprint server for biology · 2025Article
- Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Divergent Key Residues of TwoMicroorganisms · 2021Article
- Engineered chemotaxis core signaling units indicate a constrained kinase-off state.Science signaling · 2020Article
- Regulation of the chemotaxis histidine kinase CheA: A structural perspective.Biochimica et biophysica acta. Biomembranes · 2020Review
- Identification of a Kinase-Active CheA Conformation in Escherichia coli Chemoreceptor Signaling Complexes.Journal of bacteriology · 2019Article
- Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.Scientific reports · 2017Article
- Phosphoryl Group Flow within the Pseudomonas aeruginosa Pil-Chp Chemosensory System: DIFFERENTIAL FUNCTION OF THE EIGHT PHOSPHOTRANSFERASE AND THREE RECEIVER DOMAINS.The Journal of biological chemistry · 2016Article
- Conformational Transitions that Enable Histidine Kinase Autophosphorylation and Receptor Array Integration.Journal of molecular biology · 2015Article
- Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update.Trends in microbiology · 2015Review
- Architecture and signal transduction mechanism of the bacterial chemosensory array: progress, controversies, and challenges.Current opinion in structural biology · 2014Review
- Article
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3 authors.
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Abstract
The histidine autokinase CheA functions as the central processing unit in the Escherichia coli chemotaxis signaling machinery. CheA receives autophosphorylation control inputs from chemoreceptors and in turn regulates the flux of signaling phosphates to the CheY and CheB response regulator proteins. Phospho-CheY changes the direction of flagellar rotation; phospho-CheB covalently modifies receptor molecules during sensory adaptation. The CheA phosphorylation site, His-48, lies in the N-terminal P1 domain, which must engage the CheA ATP-binding domain, P4, to initiate an autophosphorylation reaction cycle. The docking determinants for the P1-P4 interaction have not been experimentally identified. We devised mutant screens to isolate P1 domains with impaired autophosphorylation or phosphotransfer activities. One set of P1 mutants identified amino acid replacements at surface-exposed residues distal to His-48. These lesions reduced the rate of P1 transphosphorylation by P4. However, once phosphorylated, the mutant P1 domains transferred phosphate to CheY at the wild-type rate. Thus, these P1 mutants appear to define interaction determinants for P1-P4 docking during the CheA autophosphorylation reaction.
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