Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate.

Abstract:

:The cheA gene encodes two overlapping polypeptides with a common carboxyl terminus: CheAL and CheAS. CheAL plays a central role in the Escherichia coli chemotaxis signalling pathway by autophosphorylation and transferring the phosphate to both CheY and CheB. On the other hand, the physiological functions of CheAS remain unknown. We have observed that overproduction of CheAS in wild-type cells increased counterclockwise-biased flagellar rotation, and this effect is dependent on the presence of CheZ. CheZ specifically facilitates CheY-phosphate (CheY-P) dephosphorylation and generates a smooth swimming signal. A physical interaction was detected between CheZ and CheAS in wild-type cell lysates by immunoprecipitation. The CheAS/CheZ interaction does not require other chemotaxis components, as we could form the complex using purified CheAS and CheZ proteins. The ability of CheAS to bind to CheZ depends on its being in the reduced state. We found that under non-reducing conditions, CheAS appears to form intermolecular disulphide bonds and loses the ability to bind to CheZ. Finally, the CheAS/CheZ complex formed in vitro shows a greater dephosphorylating activity on CheY-P than does free CheZ.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Wang H,Matsumura P

doi

10.1046/j.1365-2958.1996.393934.x

subject

Has Abstract

pub_date

1996-02-01 00:00:00

pages

695-703

issue

4

eissn

0950-382X

issn

1365-2958

journal_volume

19

pub_type

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