Open AccessStabilization of the phosphorylated form of Bacillus subtilis DegU caused by degU9 mutation
Author(s) -
Tanaka Teruo,
KawataMukai Mutsumi
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06620.x
Subject(s) - phosphorylation , bacillus subtilis , overproduction , dephosphorylation , mutant , mutation , response regulator , biology , biochemistry , protein phosphorylation , wild type , phosphate , regulator , chemistry , microbiology and biotechnology , bacteria , gene , phosphatase , genetics , protein kinase a
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.