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Effect of D-Lactate on the Physiological Activity of the ArcB Sensor Kinase in Escherichia coli

Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, 04510 Mexico City, Mexico,¹ Laboratory of Metabolic Engineering, Korea Research Institute of Bioscience and Biotechnology, 52 Oun-dong, Yusong-gu, Daejeon 305-333, Korea²

Received 6 October 2003/ Accepted 16 December 2003

The Arc two-component system, comprising the ArcB sensor kinase and the ArcA response regulator, modulates the expression of numerous genes in response to the respiratory growth conditions. Under anoxic growth conditions ArcB autophosphorylates and transphosphorylates ArcA, which in turn represses or activates its target operons. The anaerobic metabolite D-lactate has been shown to stimulate the in vitro autophosphorylating activity of ArcB. In this study, the in vivo effect of D-lactate on the kinase activity of ArcB was assessed. The results demonstrate that D-lactate does not act as a direct signal for activation of ArcB, as previously proposed, but acts as a physiologically significant effector that amplifies ArcB kinase activity.

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