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Several enzymes of the central metabolism are phosphorylated in Staphylococcus aureus
Author(s) -
LomasLopez Rodrigo,
Paracuellos Patricia,
Riberty Mylène,
Cozzone Alain J.,
Duclos Bertrand
Publication year - 2007
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.1574-6968.2007.00742.x
Subject(s) - phosphorylation , serine , biochemistry , kinase , enzyme , biology , threonine , protein phosphorylation , virulence , staphylococcus aureus , glycolysis , protein serine threonine kinases , microbiology and biotechnology , protein kinase a , bacteria , gene , genetics
Staphylococcus aureus is an important human and animal pathogen that harbors protein kinases. The proteins phosphorylated in this bacterium grown on glucose minimal medium have been in vivo labeled with[ 32 P]‐orthophosphate and analyzed by two‐dimensional gel electrophoresis followed by MS. A total of 11 glycolytic phosphoproteins have been identified and verified. In vitro analyses have revealed that phosphorylation of these glycolytic enzymes is catalysed primarily through the activity of an endogenous serine/threonine kinase and to a lesser extent by a tyrosine kinase. The identification of these phosphoproteins should prove helpful in understanding and unravelling of the role of phosphorylation with respect to pathogenesis and virulence in this organism.

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