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A novel protein kinase that controls carbon catabolite repression in bacteria
Author(s) -
Reizer Jonathan,
Hoischen Christian,
Titgemeyer Friedrich,
Rivolta Carlo,
Rabus Ralf,
Stülke Jörg,
Karamata Dimitri,
Saier Jr Milton H.,
Hillen Wolfgang
Publication year - 1998
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1998.00747.x
Subject(s) - catabolite repression , pep group translocation , biology , biochemistry , bacillus subtilis , protein kinase a , fed batch culture , phosphorylation , kinase , bacteria , mutant , gene , genetics , fermentation
HPr(Ser) kinase is the sensor in a multicomponent phosphorelay system that controls catabolite repression, sugar transport and carbon metabolism in Gram‐positive bacteria. Unlike most other protein kinases, it recognizes the tertiary structure in its target protein, HPr, a phosphocarrier protein of the bacterial phosphotransferase system and a transcriptional cofactor controlling the phenomenon of catabolite repression. We have identified the gene ( ptsK ) encoding this serine/threonine protein kinase and characterized the purified protein product. Orthologues of PtsK have been identified only in bacteria. These proteins constitute a novel family unrelated to other previously characterized protein phosphorylating enzymes. The Bacillus subtilis kinase is shown to be allosterically activated by metabolites such as fructose 1,6‐bisphosphate and inhibited by inorganic phosphate. In contrast to wild‐type B. subtilis , the ptsK mutant is insensitive to transcriptional regulation by catabolite repression. The reported results advance our understanding of phosphorylation‐dependent carbon control mechanisms in Gram‐positive bacteria.