ISSN:
0570-0833
Keywords:
Protein phosphorylation
;
Phosphorylation
;
Bacteria
;
Gene expression
;
Metabolism
;
Chemistry
;
General Chemistry
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The importance of protein phosphorylation to the regulation of physiological processes in eukaryotic cells has been known for almost half a century. In contrast, the first conclusive evidence for functionally relevant protein phosphorylation in bacteria was obtained less than a decade ago. To date, only five functionally well-characterized bacterial proteins have been shown to be regulated by reversible phosphorylation. (1) Phosphorylation of isocitrate dehydrogenase in Escherichia coli controls the relative flux of carbon through the Krebs cycle and the glyoxylate shunt. (2) In gram-positive bacteria, phosphorylation of HPr, a phosphoryl carrier protein of the phosphoenolypyruvate-dependent sugar phosphotransferase system, regulates carbohydrate uptake via this system. (3) Phosphorylation of glycerol kinase in Streptococcus faecalis probably serves to regulate the degradation of glycerol. (4) Phosphorylation of the nitrogen regulatory protein I (NR1) in E. coli controls expression of genes encoding the enzymes which participate in nitrogen metabolism. (5) Phosphorylation of citrate lyase ligase in Clostridium sphenoides regulates the conversion of citrate lyase from the inactive sulfhydryl form to the active acetylated form. Recent investigations have shown that more than one hundred proteins in E. coli are phosphorylated. It can therefore be anticipated that protein phosphorylation will prove to be as important to the regulation of physiological processes in bacteria as it is in eukaryotes.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/anie.198810401
Permalink
