Degradation of a Caulobacter soluble cytoplasmic chemoreceptor is ClpX dependent
| Autor: | Magne Østerås, Melanie Thein, Isabel Potocka, M. R. K. Alley, Urs Jenal |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Cytoplasm
Proteolysis Molecular Sequence Data Methyl-Accepting Chemotaxis Proteins Genetics and Molecular Biology MCPB Microbiology chemistry.chemical_compound Bacterial Proteins Caulobacter crescentus medicine Amino Acid Sequence Molecular Biology Peptide sequence Adenosine Triphosphatases medicine.diagnostic_test biology Methyl-accepting chemotaxis protein C-terminus Chemotaxis Escherichia coli Proteins Cell Cycle Membrane Proteins Endopeptidase Clp Gene Expression Regulation Bacterial biology.organism_classification AAA proteins Chemoreceptor Cells Biochemistry chemistry Solubility ATPases Associated with Diverse Cellular Activities Molecular Chaperones |
| Zdroj: | Journal of bacteriology. 184(23) |
| ISSN: | 0021-9193 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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