| Autor: |
Tanaka, Teruo, Kawata-Mukai, Mutsumi |
| Zdroj: |
FEMS Microbiology Letters; January 1994, Vol. 115 Issue: 1 p93-93, 1p |
| Abstrakt: |
A Bacillus subtilis response regulator, DegU9, carrying an amino acid alteration caused by the degU9(Hy) mutation was partially purified, and phosphorylation and dephosphorylation of the protein was studied. The extent of phosphorylation was not as high as the level attained with wild-type DegU, but the DegU9-phosphate once formed was more stable than the wild-type DegU-phosphate. An in vivo study with a degU9 mutant showed that degS was necessary for the overproduction of exoproteases. These results suggest that phosphorylation is necessary for the mutant DegU9 to exert its effect and that the higher stability of phosphorylated DegU9 is responsible for the overproulation phenotype. |
| Databáze: |
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