Purification and in vitro phosphorylation of Myxococcus xanthus AsgA protein.
AUTOR(ES)
Li, Y
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=177652Documentos Relacionados
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