Ser/Thr/Tyr Protein Phosphorylation in Bacteria – For Long Time Neglected, Now Well EstablishedDeutscher J.a · Saier Jr. M.H.b
aMicrobiologie et Génétique Moléculaire, CNRS/INRA/INA-PG UMR2585, Thiverval-Grignon, France; bDivision of Biological Sciences, University of California at San Diego, La Jolla, Calif., USA
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The first clearly established example of Ser/Thr/Tyr phosphorylation of a bacterial protein was isocitrate dehydrogenase. In 1979, 25 years after the discovery of protein phosphorylation in eukaryotes, this enzyme was reported to become phosphorylated on a serine residue. In subsequent years, numerous other bacterial proteins phosphorylated on Ser, Thr or Tyr were discovered and the corresponding protein kinases and P-protein phosphatases were identified. These protein modifications regulate all kinds of physiological processes. Ser/Thr/Tyr phosphorylation in bacteria therefore seems to play a similar important role as in eukaryotes. Surprisingly, many bacterial protein kinases do not exhibit any similarity to eukaryotic protein kinases, but rather resemble nucleotide-binding proteins or kinases phosphorylating diverse low-molecular-weight substrates.
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