Purification and in vitro phosphorylation of Myxococcus xanthus AsgA protein.
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.
Department of Biology, Texas A&M University, College Station 77843-3258, USA.
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Li
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Plamann
D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics; D006639:Histidine / Q000378:metabolism; D008345:Manganese / Q000494:pharmacology; D008969:Molecular Sequence Data; D016941:Myxococcus xanthus / Q000737:chemistry*; D010766:Phosphorylation / Q000187:drug effects; D010770:Phosphotransferases; D011494:Protein Kinases / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000302:isolation & purification
D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D008345:Manganese; D006639:Histidine; D010770:Phosphotransferases; D011494:Protein Kinases; C093119:AsgA protein, Myxococcus xanthus