Potocka, Isabel Thein, Melanie Østerås, Magne Jenal, Urs Alley, M. R. K. <jats:title>ABSTRACT</jats:title> <jats:p>In order to determine whether ClpXP-mediated proteolysis is a common mechanism used to regulate the chemotaxis machinery during the cell cycle of <jats:italic>Caulobacter crescentus</jats:italic>, we have characterized a soluble cytoplasmic chemoreceptor, McpB. The <jats:italic>mcpB</jats:italic> 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.</jats:p> application/pdf https://sonar.ch/global/documents/11265 eng info:eu-repo/semantics/altIdentifier/doi/10.1128/jb.184.23.6635-6642.2002 info:eu-repo/semantics/altIdentifier/issn/0021-9193 info:eu-repo/semantics/openAccess Journal of Bacteriology. - American Society for Microbiology. - 2002, vol. 184, no. 23, p. 6635-6641 Molecular Biology Microbiology Degradation of a Caulobacter Soluble Cytoplasmic Chemoreceptor Is ClpX Dependent http://purl.org/coar/resource_type/c_6501