ArticleNature communications2020
Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
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- Metal Messengers: Communication in the Bacterial World through Transition-Metal-Sensing Two-Component Systems.Biochemistry · 2023Review
- Anti-Virulence Strategy of Novel Dehydroabietic Acid Derivatives: Design, Synthesis, and Antibacterial Evaluation.International journal of molecular sciences · 2023Article
- Phosphorylation chemistry of the Bordetella PlrSR TCS and its contribution to bacterial persistence in the lower respiratory tract.Molecular microbiology · 2023Article
- Identification of an antivirulence agent targeting the master regulator of virulence genes inFrontiers in cellular and infection microbiology · 2023Article
- Single-molecule studies reveal method for tuning the heterogeneous activity of alkaline phosphatase.Biophysical journal · 2022Article
- Polymyxin Resistance in Clinical Isolates ofFrontiers in cellular and infection microbiology · 2022Article
- Diversity in Sensing and Signaling of Bacterial Sensor Histidine Kinases.Biomolecules · 2021Review
- Article
- The CckA-ChpT-CtrA Phosphorelay Controlling Rhodobacter capsulatus Gene Transfer Agent Production Is Bidirectional and Regulated by Cyclic di-GMP.Journal of bacteriology · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Histidine is a versatile residue playing key roles in enzyme catalysis thanks to the chemistry of its imidazole group that can serve as nucleophile, general acid or base depending on its protonation state. In bacteria, signal transduction relies on two-component systems (TCS) which comprise a sensor histidine kinase (HK) containing a phosphorylatable catalytic His with phosphotransfer and phosphatase activities over an effector response regulator. Recently, a pH-gated model has been postulated to regulate the phosphatase activity of HisKA HKs based on the pH-dependent rotamer switch of the phosphorylatable His. Here, we have revisited this model from a structural and functional perspective on HK853-RR468 and EnvZ-OmpR TCS, the prototypical HisKA HKs. We have found that the rotamer of His is not influenced by the environmental pH, ruling out a pH-gated model and confirming that the chemistry of the His is responsible for the decrease in the phosphatase activity at acidic pH.
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