ArticleJournal of bacteriology2008
Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 66 citations in OpenAlex.
- Bacterial Chemoreceptors Transmit Stimulus Signals Through Coupled Entropic Switches.Journal of molecular biology · 2026Article
- AlphaFold2 captures the conformational landscape of the HAMP signaling domain.Protein science : a publication of the Protein Society · 2024Article
- New Roles for HAMP Domains: the Tri-HAMP Region of Pseudomonas aeruginosa Aer2 Controls Receptor Signaling and Cellular Localization.Journal of bacteriology · 2022Article
- 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
- Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity.International journal of molecular sciences · 2021Review
- Directed evolution reveals the mechanism of HitRS signaling transduction in Bacillus anthracis.PLoS pathogens · 2020Article
- Structure and function of the juxtamembrane GAF domain of potassium biosensor KdpD.Protein science : a publication of the Protein Society · 2020Article
- Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain.Nature communications · 2020Article
- 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
- 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
- Evidence for a Helix-Clutch Mechanism of Transmembrane Signaling in a Bacterial Chemoreceptor.Journal of molecular biology · 2016Article
- Signaling and Adaptation Modulate the Dynamics of the Photosensoric Complex of Natronomonas pharaonis.PLoS computational biology · 2015Article
- A Trigger Residue for Transmembrane Signaling in the Escherichia coli Serine Chemoreceptor.Journal of bacteriology · 2015Article
- Signal transduction in histidine kinases: insights from new structures.Structure (London, England : 1993) · 2015Review
- Article
- Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update.Trends in microbiology · 2015Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
HAMP domains are approximately 50-residue motifs, found in many bacterial signaling proteins, that consist of two amphiphilic helices joined by a nonhelical connector segment. The HAMP domain of Tsr, the serine chemoreceptor of Escherichia coli, receives transmembrane input signals from the periplasmic serine binding domain and in turn modulates output signals from the Tsr kinase control domain to elicit chemotactic responses. We created random amino acid replacements at each of the 14 connector residues of Tsr-HAMP to identify those that are critical for Tsr function. In all, we surveyed 179 connector missense mutants and identified three critical residues (G235, L237, and I241) at which most replacements destroyed Tsr function and another important residue (G245) at which most replacements impaired Tsr function. The region surrounding G245 tolerated 1-residue deletions and insertions of up to 10 glycines, suggesting a role as a relatively nonspecific, flexible linker. The critical connector residues are consistent with a structural model of the Tsr-HAMP domain based on the solution structure of an isolated thermophile HAMP domain (M. Hulko, F. Berndt, M. Gruber, J. U. Linder, V. Truffault, A. Schultz, J. Martin, J. E. Schultz, A. N. Lupas, and M. Coles, Cell 126:929-940, 2006) in which G235 defines a critical turn at the C terminus of the first helix and L237 and I241 pack against the helices, perhaps to stabilize alternative HAMP signaling conformations. Most I241 lesions locked Tsr signal output in the kinase-on mode, implying that this residue is responsible mainly for stabilizing the kinase-off signaling state. In contrast, lesions at L237 resulted in a variety of aberrant output patterns, suggesting a role in toggling output between signaling states.
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