ArticleBiophysical journal2012
Self-association of the histidine kinase CheA as studied by pulsed dipolar ESR spectroscopy.
Article in Biophysical journal, 2012. 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, 23 citations in OpenAlex.
- Localized Reconstruction of Multimodal Distance Distribution from DEER Data of Biopolymers.bioRxiv : the preprint server for biology · 2025Article
- Engineered chemotaxis core signaling units indicate a constrained kinase-off state.Science signaling · 2020Article
- Inhibiting the copper efflux system in microbes as a novel approach for developing antibiotics.PloS one · 2019Article
- Exploring the role of the various methionine residues in the Escherichia coli CusB adapter protein.PloS one · 2019Article
- Site-Specific Incorporation of a CuThe journal of physical chemistry. B · 2018Article
- The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations.Protein science : a publication of the Protein Society · 2017Article
- Stability and Conformation of a Chemoreceptor HAMP Domain Chimera Correlates with Signaling Properties.Biophysical journal · 2017Article
- Bacterial Energy Sensor Aer Modulates the Activity of the Chemotaxis Kinase CheA Based on the Redox State of the Flavin Cofactor.The Journal of biological chemistry · 2016Article
- Detection of Ligand-induced Conformational Changes in the Activation Loop of Aurora-A Kinase by PELDOR Spectroscopy.ChemistryOpen · 2016Article
- Conformational Response of Influenza A M2 Transmembrane Domain to Amantadine Drug Binding at Low pH (pH 5.5).Frontiers in physiology · 2016Article
- Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes.Scientific reports · 2015Article
- Room-temperature distance measurements of immobilized spin-labeled protein by DEER/PELDOR.Biophysical journal · 2015Article
- Taking the pulse of protein interactions by EPR spectroscopy.Biophysical journal · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Biologically important protein complexes often involve molecular interactions that are low affinity or transient. We apply pulsed dipolar electron spin resonance spectroscopy and site-directed spin labeling in what to our knowledge is a new approach to study aggregation and to identify regions on protein surfaces that participate in weak, but specific molecular interactions. As a test case, we have probed the self-association of the chemotaxis kinase CheA, which forms signaling clusters with chemoreceptors and the coupling protein CheW at the poles of bacterial cells. By measuring the intermolecular dipolar interactions sensed by spin-labels distributed over the protein surface, we show that the soluble CheA kinase aggregates to a small extent through interactions mediated by its regulatory (P5) domain. Direct dipolar distance measurements confirm that a hydrophobic surface at the periphery of P5 subdomain 2 associates CheA dimers in solution. This result is further supported by differential disulfide cross-linking from engineered cysteine reporter sites. We suggest that the periphery of P5 is an interaction site on CheA for other similar hydrophobic surfaces and plays an important role in structuring the signaling particle.
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