J. Bacteriol., Jan 1996, 289-292, Vol 178, No. 1
Copyright © 1996, American Society for Microbiology

Purification and in vitro phosphorylation of Myxococcus xanthus AsgA protein

Y Li and L Plamann
Department of Biology, Texas A&M University, College Station 77843- 3258, USA.

The deduced amino acid sequence of the Myxococcus xanthus AsgA protein contains an N-terminal domain that is homologous to the receiver of response regulators and a C-terminal domain that is homologous to the transmitter of histidine protein kinases. We overexpressed affinity- tagged AsgA in Escherichia coli, purified the recombinant protein, and showed that AsgA has autokinase activity in vitro. The results of chemical-stability assays suggest that AsgA is phosphorylated on a histidine and provide no evidence for transfer of the phosphoryl group to the conserved aspartate of the receiver domain.

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