PMID:19851741
| Citation |
Liu, X, Peña Sandoval, GR, Wanner, BL, Jung, WS, Georgellis, D and Kwon, O (2009) Evidence against the physiological role of acetyl phosphate in the phosphorylation of the ArcA response regulator in Escherichia coli. J. Microbiol. 47:657-62 |
|---|---|
| Abstract |
The Arc two-component signal transduction system of Escherichia coli comprises the ArcB sensor kinase and the ArcA response regulator. Under anoxic growth conditions, ArcB autophosphorylates and transphos-phorylates ArcA, which, in turn, represses or activates its target operons. ArcA has been shown to be able to autophosphorylate in vitro at the expense of acetyl-P. Here, the in vivo effect of acetyl phosphate on the redox signal transduction by the Arc system was assessed. Our results indicate that acetyl phosphate can modulate the expression of ArcA-P target genes only in the absence of ArcB. Therefore, the acetyl phosphate dependent ArcA phosphorylation route does not seem to play a significant role under physiological conditions. |
| Links |
PubMed Online version:10.1007/s12275-009-0087-9 |
| Keywords |
Bacterial Outer Membrane Proteins/metabolism; Escherichia coli/physiology; Escherichia coli Proteins/metabolism; Models, Biological; Organophosphates/metabolism; Phosphorylation; Repressor Proteins/metabolism |
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