Ser/Thr/Tyr Protein Phosphorylation in Bacteria – For Long Time Neglected, Now Well EstablishedDeutscher J. · Saier Jr. M.H.
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
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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Number of Print Pages : 7
Number of Figures : 0, Number of Tables : 0, Number of References : 83
Journal of Molecular Microbiology and Biotechnology
Vol. 9, No. 3-4, Year 2005 (Cover Date: January 2006)
Journal Editor: Saier, M.H., Jr. (La Jolla, Calif.)
ISSN: 1464–1801 (print), 1660–2412 (Online)
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