Tanabe H, Masuda T, Yamasaki K, Katoh A, Yoshioka S, Utsumi R
Department of Agricultural Chemistry, Kinki University, Nara, Japan.
Biosci Biotechnol Biochem. 1998 Jan;62(1):78-82. doi: 10.1271/bbb.62.78.
EvgA and EvgS constitute one two-component signal transduction system in Escherichia coli. Although probable signaling domains of these proteins have been estimated, the molecular mechanism of their interaction remains to be elucidated. Here, we investigated protein to protein interactions between EvgA and EvgS and also between the EvgAS system and other related signaling pathways by means of surface plasmon resonance. EvgA and EvgS interacted directly and inhibition of phosphorylation of their functional domains abolished formation of the EvgAS complex. No interaction was observed either between EvgA and Bordetella BvgS or BvgA and EvgS. OmpR, a response regulator for the osmoregulative gene expression of E. coli, had similar but not identical behavior towards EvgS to that of EvgA. These results indicate that interaction between the signaling proteins is closely related to phosphorylation of the functional domain of the proteins.
EvgA和EvgS在大肠杆菌中构成一个双组分信号转导系统。尽管已经估计了这些蛋白质可能的信号结构域，但其相互作用的分子机制仍有待阐明。在此，我们通过表面等离子体共振研究了EvgA和EvgS之间以及EvgAS系统与其他相关信号通路之间的蛋白质-蛋白质相互作用。EvgA和EvgS直接相互作用，其功能结构域磷酸化的抑制消除了EvgAS复合物的形成。未观察到EvgA与博德特氏菌BvgS之间或BvgA与EvgS之间有相互作用。OmpR是大肠杆菌渗透调节基因表达的应答调节因子，其对EvgS的行为与EvgA相似但不完全相同。这些结果表明，信号蛋白之间的相互作用与蛋白质功能结构域的磷酸化密切相关。
