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- W4313702404 abstract "Abstract The major food-borne pathogen Campylobacter jejuni employs chemotactic motility to colonise the avian gut, and also as a virulence mechanism in human diarrhoeal disease. In Escherichia coli CheY activity is modulated by CheZ, a phosphatase originally thought to be absent in C. jejuni . The Hp0170 protein of Helicobacter pylori is a distant homologue of CheZ and, as C. jejuni Cj0700 is homologous to HP0170, Cj0700 could also act as a CheZ orthologue in Campylobacter . Both the C. jejuni CheV and CheA proteins also contain a response regulator (RR) domain that may be phosphorylated. Cj0700 would therefore be predicted to dephosphorylate C. jejuni CheY and possibly also the CheV and CheA RR domains. A mutant (Δ cj0700) and complement (Δ cj0700, cj0046 :: cj0700 ) were constructed in C . jejuni strains NCTC11168, NCTC11828 and 81-176. On semisolid agar the Δ cj0700 mutant strain showed reduced motility relative to wild-type and this phenotype was reversed in the complemented strain. In pull down and bacterial two hybrid assays, expressed Cj0700 was able to interact with CheY, CheA-RR and CheV. Cj0700 is able to dephosphorylate the RR domain of CheY and CheA-RR, but less efficiently, CheV. These findings verify that Cj0700 plays a role in C. jejuni chemotaxis through phosphatase activity with respect to CheY, and is hence likely to be a CheZ orthologue. Cj0700 also partially modulates the phosphorylation level of the RR domain on CheA and CheV, although the functional consequences of this interaction require further investigation." @default.
- W4313702404 created "2023-01-08" @default.
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- W4313702404 date "2023-01-07" @default.
- W4313702404 modified "2023-09-27" @default.
- W4313702404 title "A CheZ orthologue in<i>Campylobacter jejuni</i>plays a role in chemotaxis through conserved phosphatase activity" @default.
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- W4313702404 doi "https://doi.org/10.1101/2023.01.06.523011" @default.
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