Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis
| Autor: | Marta Perego, Conrad Hanstein, Philippe Glaser, James A. Hoch, Katherine M. Welsh, Tsotne Djavakhishvili |
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| Rok vydání: | 1994 |
| Předmět: |
Transcription
Genetic Molecular Sequence Data Restriction Mapping Phosphatase Regulator Sigma Factor Biology Second Messenger Systems General Biochemistry Genetics and Molecular Biology Bacterial Proteins Phosphoprotein Phosphatases Amino Acid Sequence Transcription factor Spores Bacterial Kinase fungi Cell Differentiation Gene Expression Regulation Bacterial Cell cycle DNA-Binding Proteins Response regulator Biochemistry Mutation bacteria Phosphorylation Signal transduction Bacillus subtilis Transcription Factors |
| Zdroj: | Cell. 79:1047-1055 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/0092-8674(94)90035-3 |
| Popis: | The initiation of sporulation in B. subtilis is regulated by the Spo0A transcription factor, which is activated by phosphorylation to control developmental switching from the vegetative to the sporulation state. The level of phosphorylation of Spo0A is regulated by the phosphorelay, a signal transduction system based on the protein-histidine kinase-response regulator two-component paradigm. To initiate sporulation, the cell must recognize and interpret a large variety of environmental, metabolic, and cell cycle signals that influence the phosphorylation level of Spo0A. We describe here a family of protein-aspartate phosphatases with activity on Spo0F approximately P, a response regulator component of the phosphorelay, that provide a mechanism for signal recognition and interpretation. These phosphatases function to drain the phosphorelay, lower Spo0A approximately P levels, and prevent sporulation. The integration of diverse environmental signals that affect the initiation of sporulation likely occurs through the competition between opposing activities of protein kinases and protein phosphatases. |
| Databáze: | OpenAIRE |
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