ArticleMolecular microbiology2013
Missense substitutions reflecting regulatory control of transmitter phosphatase activity in two-component signalling.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 22 citations in OpenAlex.
- Mutations in SilS and CusS/OmpC represent different routes to achieve high level silver ion tolerance in Klebsiella pneumoniae.BMC microbiology · 2022Article
- Allostery and protein plasticity: the keystones for bacterial signaling and regulation.Biophysical reviews · 2021Review
- Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity.International journal of molecular sciences · 2021Review
- Sensor Histidine Kinase NarQ Activates via Helical Rotation, Diagonal Scissoring, and Eventually Piston-Like Shifts.International journal of molecular sciences · 2020Article
- Acquired Nisin Resistance inmSphere · 2018Article
- Phosphatase activity tunes two-component system sensor detection threshold.Nature communications · 2018Article
- Conformational dynamics of the essential sensor histidine kinase WalK.Acta crystallographica. Section D, Structural biology · 2017Article
- Cross Talk Inhibition Nullified by a Receiver Domain Missense Substitution.Journal of bacteriology · 2015Article
- Sensor-response regulator interactions in a cross-regulated signal transduction network.Microbiology (Reading, England) · 2015Article
- Functional characterization of WalRK: A two-component signal transduction system from Bacillus anthracis.FEBS open bio · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Negative control in two-component signal transduction results from sensor transmitter phosphatase activity for phospho-receiver dephosphorylation. A hypothetical mechanism for this reaction involves a catalytic residue in the H-box active-site region. However, a complete understanding of transmitter phosphatase regulation is hampered by the abundance of kinase-competent, phosphatase-defective missense substitutions (K(+) P(-) phenotype) outside of the active-site region. For the Escherichia coli NarX sensor, a model for the HisKA_3 sequence family, DHp domain K(+) P(-) mutants defined two classes. Interaction mutants mapped to the active site-distal base of the DHp helix 1, whereas conformation mutants were affected in the X-box region of helix 2. Thus, different types of perturbations can influence transmitter phosphatase activity indirectly. By comparison, K(+) P(-) substitutions in the HisKA sensors EnvZ and NtrB additionally map to a third region, at the active site-proximal top of the DHp helix 1, independently identified as important for DHp-CA domain interaction in this sensor class. Moreover, the NarX transmitter phosphatase activity was independent of nucleotides, in contrast to the activity for many HisKA family sensors. Therefore, distinctions involving both the DHp and the CA domains suggest functional diversity in the regulation of HisKA and HisKA_3 transmitter phosphatase activities.
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