CheX in the Three-Phosphatase System of Bacterial Chemotaxis
| Autor: | George W. Ordal, Richard M. Foster, Peter J. Y. Liu, Travis J. Muff |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Phosphatase
Motility Heterologous Bacillus subtilis medicine.disease_cause Models Biological Microbiology Bacterial Proteins Phosphoprotein Phosphatases medicine Molecular Biology Escherichia coli biology Chemotaxis Gene Expression Regulation Bacterial biology.organism_classification Response regulator Biochemistry Flagella Mutation bacteria Bacteria Protein Binding Signal Transduction |
| Zdroj: | Journal of Bacteriology. 189:7007-7013 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.00896-07 |
| Popis: | Bacterial chemotaxis involves the regulation of motility by a modified two-component signal transduction system. In Escherichia coli , CheZ is the phosphatase of the response regulator CheY but many other bacteria, including Bacillus subtilis , use members of the CheC-FliY-CheX family for this purpose. While Bacillus subtilis has only CheC and FliY, many systems also have CheX. The effect of this three-phosphatase system on chemotaxis has not been studied previously. CheX was shown to be a stronger CheY-P phosphatase than either CheC or FliY. In Bacillus subtilis , a cheC mutant strain was nearly complemented by heterologous cheX expression. CheX was shown to overcome the Δ cheC adaptational defect but also generally lowered the counterclockwise flagellar rotational bias. The effect on rotational bias suggests that CheX reduced the overall levels of CheY-P in the cell and did not truly replicate the adaptational effects of CheC. Thus, CheX is not functionally redundant to CheC and, as outlined in the discussion, may be more analogous to CheZ. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|