PMID:10585483
| Citation |
Georgellis, D, Kwon, O and Lin, EC (1999) Amplification of signaling activity of the arc two-component system of Escherichia coli by anaerobic metabolites. An in vitro study with different protein modules. J. Biol. Chem. 274:35950-4 |
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| Abstract |
In Escherichia coli, changes in redox condition of growth are sensed and signaled by the Arc two-component system. This system consists of ArcB as the membrane-associated sensor kinase and ArcA as the cytoplasmic response regulator. ArcB is a tripartite kinase, possessing a primary transmitter, a receiver, and a secondary transmitter domain that catalyzes the phosphorylation of ArcA via a His --> Asp --> His --> Asp phosphorelay, as well as the dephosphorylation of ArcA-P by a reverse phosphorelay. When ArcA and ArcB were incubated with ATP, the peak levels of phosphorylated proteins increased in the presence of the fermentation metabolites D-lactate, acetate, or pyruvate. In this study, we report that these effectors accelerate the autophosphorylation activity of ArcB and enhance the transphosphorylation of ArcA, but have no effect on the dephosphorylation of ArcA-P. Moreover, the presence of the receiver domain of ArcB is essential for the effectors to influence the autophosphorylation rate of the primary transmitter domain of ArcB. |
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| Keywords |
Acetates/metabolism; Anaerobiosis; Aspartic Acid/metabolism; Bacterial Outer Membrane Proteins/metabolism; Bacterial Proteins/metabolism; Cell Membrane/physiology; Escherichia coli/growth & development; Escherichia coli/physiology; Escherichia coli Proteins; Fermentation; Histidine/metabolism; Kinetics; Lactates/metabolism; Membrane Proteins/metabolism; Oxidation-Reduction; Phosphoric Monoester Hydrolases/metabolism; Phosphorylation; Protein Kinases; Pyruvates/metabolism; Repressor Proteins; Signal Transduction |
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