ArticleProceedings of the National Academy of Sciences of the United States of America2010
Conserved mechanism for sensor phosphatase control of two-component signaling revealed in the nitrate sensor NarX.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
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- Marginal specificity in protein interactions constrains evolution of a paralogous family.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Rvv two-component regulatory system regulates biofilm formation and colonization in Vibrio cholerae.PLoS pathogens · 2023Article
- Phosphorylation chemistry of the Bordetella PlrSR TCS and its contribution to bacterial persistence in the lower respiratory tract.Molecular microbiology · 2023Article
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- Real-time detection of response regulator phosphorylation dynamics in live bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Three Orphan Histidine Kinases Inhibit Clostridioides difficile Sporulation.Journal of bacteriology · 2022Article
- Robust and tunable signal processing in mammalian cells via engineered covalent modification cycles.Nature communications · 2022Article
- The W-Acidic Motif of Histidine Kinase WalK Is Required for Signaling and Transcriptional Regulation inFrontiers in microbiology · 2022Article
- The Impact of Omega-3 Fatty Acids on the Evolution of Acinetobacter baumannii Drug Resistance.Microbiology spectrum · 2021Article
- Hybrid Histidine Kinase BinK Represses Vibrio fischeri Biofilm Signaling at Multiple Developmental Stages.Journal of bacteriology · 2021Article
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3 authors.
Funding
Abstract
Two-component signal transduction mediates a wide range of phenotypes in microbes and plants. The sensor transmitter module controls the phosphorylation state of the cognate-response-regulator receiver domain. Whereas the two-component autokinase and phosphotransfer reactions are well-understood, the mechanism by which sensors accelerate the rate of phospho-response regulator dephosphorylation, termed "transmitter phosphatase activity," is unknown. We identified a conserved DxxxQ motif adjacent to the phospho-accepting His residue in the HisKA_3 subfamily of two-component sensors. We used site-specific mutagenesis to make substitutions for these conserved Gln and Asp residues in the nitrate-responsive NarX sensor and analyzed function both in vivo and in vitro. Results show that the Gln residue is critical for transmitter phosphatase activity, but is not essential for autokinase or phosphotransfer activities. The documented role of an amide moiety in phosphoryl group hydrolysis suggests an analogous catalytic function for this Gln residue in HisKA_3 members. Results also indicate that the Asp residue is important for both autokinase and transmitter phosphatase activities. Furthermore, we noted that sensors of the HisKA subfamily exhibit an analogous E/DxxT/N motif, the conserved Thr residue of which is critical for transmitter phosphatase activity of the EnvZ sensor. Thus, two-component sensors likely use similar mechanisms for receiver domain dephosphorylation.
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