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Journal of Bacteriology, December 2002, p. 6635-6641, Vol. 184, No. 23
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.23.6635-6642.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Degradation of a Caulobacter Soluble Cytoplasmic Chemoreceptor Is ClpX Dependent

Isabel Potocka,1 Melanie Thein,1 Magne Østerås,2 Urs Jenal,2 and M. R. K. Alley1*

Department of Biological Sciences, South Kensington Campus, Imperial College of Science, Technology and Medicine, London SW7 2AY, United Kingdom,1 Division of Molecular Microbiology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland2

Received 5 June 2002/ Accepted 23 August 2002

In order to determine whether ClpXP-mediated proteolysis is a common mechanism used to regulate the chemotaxis machinery during the cell cycle of Caulobacter crescentus, we have characterized a soluble cytoplasmic chemoreceptor, McpB. The mcpB gene lies adjacent to the major chemotaxis operon, which encodes 12 chemotaxis proteins, including the membrane chemoreceptor McpA. Like McpA, McpB possesses a C-terminal CheBR docking motif and three potential methylation sites, which we suggest are methylated. The McpB protein is degraded via a ClpX-dependent pathway during the swarmer-to-stalked cell transition, and a motif, which is 3 amino acids N-terminal to the McpB CheBR docking site, is required for proteolysis. Analysis of the degradation signal in McpB and McpA reveals a common motif present in the other four chemoreceptors that possess CheBR docking sites. A green fluorescent protein (GFP) fusion bearing 58 amino acids from the C terminus of McpA, which contains this motif, is degraded, suggesting that the C-terminal sequence is sufficient to confer ClpXP protease susceptibility.


* Corresponding author. Mailing address: Department of Biological Sciences, Biochemistry Building, South Kensington Campus, Imperial College of Science, Technology and Medicine, London SW7 2AY, United Kingdom. Phone: 020 7594 5304. Fax: 020 7594 5207. E-mail: d.alley{at}ic.ac.uk.


Journal of Bacteriology, December 2002, p. 6635-6641, Vol. 184, No. 23
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.23.6635-6642.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




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