A remote CheZ orthologue retains phosphatase function.
A remote CheZ orthologue retains phosphatase function.
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DOI：
10.1111/j.1365-2958.2010.07200.x
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发表时间：
2010-07-01
影响因子：
3.6
通讯作者：
Ottemann KM
中科院分区：
文献类型：
--
作者：
Lertsethtakarn P;Ottemann KM
Aspartyl-phosphate phosphatases underlie the rapid responses of bacterial chemotaxis. One such phosphatase, CheZ, was originally proposed to be restricted to proteobacter, suggesting only a small subset of microbes relied on this protein. A putative CheZ phosphatase was identified genetically in the epsilon proteobacter Helicobacter pylori (, Mol Micro 61:187). H. pylori utilizes a chemotaxis system consisting of CheAY, three CheVs, CheW, CheY and the putative CheZ to colonize the host stomach. Here we investigate whether this CheZ has phosphatase activity. We phosphorylated potential targets in vitro using either a phosphodonor or the CheAY kinase and [γ-32P] ATP, and found that H. pylori CheZ (CheZHP) efficiently dephosphorylates CheYHP and CheAY and has additional weak activity on CheV2. We detected no phosphatase activity toward CheV1 or CheV3. Mutations corresponding to E. coli CheZ active site residues or deletion of the C-terminal region inactivate CheZHP phosphatase activity, suggesting the two CheZ's function similarly. Bioinformatics analysis suggests that CheZ phosphatases are found in all proteobacteria classes, as well as classes Aquificae, Deferribacteres, Nitrospira, and Sphingobacteria, demonstrating that CheZ phosphatases are broadly distributed within Gram-negative bacteria.
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