黄色粘球菌AsgA蛋白的纯化及体外磷酸化
Purification and in vitro phosphorylation of Myxococcus xanthus AsgA protein.
作者信息
Li Y, Plamann L
机构信息
Department of Biology, Texas A&M University, College Station 77843-3258, USA.
出版信息
J Bacteriol. 1996 Jan;178(1):289-92. doi: 10.1128/jb.178.1.289-292.1996.
Abstract
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.
摘要
黄色粘球菌AsgA蛋白推导的氨基酸序列包含一个与应答调节因子的受体同源的N端结构域和一个与组氨酸蛋白激酶的传递器同源的C端结构域。我们在大肠杆菌中过表达了带有亲和标签的AsgA，纯化了重组蛋白，并表明AsgA在体外具有自激酶活性。化学稳定性分析结果表明AsgA在组氨酸上被磷酸化，且没有提供磷酸基团转移至受体结构域保守天冬氨酸的证据。
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