| Title |
NOTE] Evidence Against the Physiological Role of Acetyl Phosphate in the Phosphorylation of the ArcA Response Regulator in Escherichia coli |
| Author |
Xueqiao Liu1, Gabriela R. Peña Sandoval2, Barry L. Wanner3, Won Seok Jung4, Dimitris Georgellis2, and Ohsuk Kwon4* |
| Address |
1Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA, 2Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, 04510 Mexico City, Mexico, 3Department of Biological Sciences, Purdue University, Lafayette, IN 47907, USA, 4Integrative Omics Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-333, Republic of Korea |
| Bibliography |
Journal of Microbiology, 47(5),657-662, 2009,
|
| DOI |
|
| Key Words |
acetyl phosphate, Arc two-component signal transduction, ArcA response regulator, E. coli |
| 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 transphosphorylates 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. |
