A CheZ orthologue inCampylobacter jejuniplays a role in chemotaxis through conserved phosphatase activity

Author:

Jama Abdullahi S.,Ketley Julian M.

Abstract

AbstractThe major food-borne pathogenCampylobacter jejuniemploys chemotactic motility to colonise the avian gut, and also as a virulence mechanism in human diarrhoeal disease.InEscherichia coliCheY activity is modulated by CheZ, a phosphatase originally thought to be absent inC. jejuni. The Hp0170 protein ofHelicobacter pyloriis a distant homologue of CheZ and, asC. jejuniCj0700 is homologous to HP0170, Cj0700 could also act as a CheZ orthologue inCampylobacter. Both theC. jejuniCheV and CheA proteins also contain a response regulator (RR) domain that may be phosphorylated. Cj0700 would therefore be predicted to dephosphorylateC. jejuniCheY and possibly also the CheV and CheA RR domains.A mutant (Δcj0700)and complement (Δcj0700, cj0046::cj0700) were constructed inC.jejunistrains NCTC11168, NCTC11828 and 81-176. On semisolid agar the Δcj0700mutant 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 inC. jejunichemotaxis 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.

Publisher

Cold Spring Harbor Laboratory

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