ArticleJournal of molecular biology2014
Functional suppression of HAMP domain signaling defects in the E. coli serine chemoreceptor.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 37 citations in OpenAlex.
- Bacterial Chemoreceptors Transmit Stimulus Signals Through Coupled Entropic Switches.Journal of molecular biology · 2026Article
- The structural logic of dynamic signaling in the Escherichia coli serine chemoreceptor.Protein science : a publication of the Protein Society · 2024Article
- The Structural Logic of Dynamic Signaling in thebioRxiv : the preprint server for biology · 2024Article
- Signal integration in chemoreceptor complexes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Discovery of a New Chemoeffector forACS bio & med chem Au · 2022Article
- Structural signatures ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Hexameric rings of the scaffolding protein CheW enhance response sensitivity and cooperativity inScience signaling · 2022Article
- Concerted Differential Changes of Helical Dynamics and Packing upon Ligand Occupancy in a Bacterial Chemoreceptor.ACS chemical biology · 2021Article
- Protein design-scapes generated by microfluidic DNA assembly elucidate domain coupling in the bacterial histidine kinase CpxA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain.Nature communications · 2020Article
- Under Elevated c-di-GMP in Escherichia coli, YcgR Alters Flagellar Motor Bias and Speed Sequentially, with Additional Negative Control of the Flagellar Regulon via the Adaptor Protein RssB.Journal of bacteriology · 2019Article
- Identification of a Kinase-Active CheA Conformation in Escherichia coli Chemoreceptor Signaling Complexes.Journal of bacteriology · 2019Article
- Conformational shifts in a chemoreceptor helical hairpin control kinase signaling inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Inverted signaling by bacterial chemotaxis receptors.Nature communications · 2018Article
- A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Noncritical Signaling Role of a Kinase-Receptor Interaction Surface in the Escherichia coli Chemosensory Core Complex.Journal of molecular biology · 2018Article
- Paradoxical enhancement of chemoreceptor detection sensitivity by a sensory adaptation enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Stability and Conformation of a Chemoreceptor HAMP Domain Chimera Correlates with Signaling Properties.Biophysical journal · 2017Article
- Signaling Consequences of Structural Lesions that Alter the Stability of Chemoreceptor Trimers of Dimers.Journal of molecular biology · 2017Article
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2 authors at 1 institution in 1 country.
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Abstract
HAMP domains play key signaling roles in many bacterial receptor proteins. The four-helix HAMP bundle of the homodimeric Escherichia coli serine chemoreceptor (Tsr) interacts with an adjoining four-helix sensory adaptation bundle to regulate the histidine autokinase CheA bound to the cytoplasmic tip of the Tsr molecule. The adaptation helices undergo reversible covalent modifications that tune the stimulus-responsive range of the receptor: unmodified E residues promote kinase-off output, and methylated E residues or Q replacements at modification sites promote kinase-on output. We used mutationally imposed adaptational modification states and cells with various combinations of the sensory adaptation enzymes, CheR and CheB, to characterize the signaling properties of mutant Tsr receptors that had amino acid replacements in packing layer 3 of the HAMP bundle and followed in vivo CheA activity with an assay based on Förster resonance energy transfer. We found that an alanine or a serine replacement at HAMP residue I229 effectively locked Tsr output in a kinase-on state, abrogating chemotactic responses. A second amino acid replacement in the same HAMP packing layer alleviated the I229A and I229S signaling defects. Receptors with the suppressor changes alone mediated chemotaxis in adaptation-proficient cells but exhibited altered sensitivity to serine stimuli. Two of the suppressors (S255E and S255A) shifted Tsr output toward the kinase-off state, but two others (S255G and L256F) shifted output toward a kinase-on state. The alleviation of locked-on defects by on-shifted suppressors implies that Tsr-HAMP has several conformationally distinct kinase-active output states and that HAMP signaling might involve dynamic shifts over a range of bundle conformations.
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