HISTIDINE PHOSPHORYLATION AND PHOSPHORYL GROUP TRANSFER IN BACTERIAL CHEMOTAXIS
HISTIDINE PHOSPHORYLATION AND PHOSPHORYL GROUP TRANSFER IN BACTERIAL CHEMOTAXIS
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DOI：
10.1038/336139a0
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发表时间：
1988-11-10
期刊：
影响因子：
64.8
通讯作者：
SIMON, MI
中科院分区：
文献类型：
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作者：
HESS, JF;BOURRET, RB;SIMON, MI
由CheA蛋白的自磷酸化引发的蛋白磷酸化级联反应可能在细菌趋化性的信号转导途径中起重要作用。CheA的蛋白水解片段不能自磷酸化，但仍然可以将磷酸盐转移到产生兴奋和适应信号的蛋白质上。CheA磷酸化位点为His 48；在这个位置发生改变的突变体是非趋化性的。类似的瞬时蛋白磷酸化和磷酸化基团转移机制似乎涉及处理感官数据和激活特定基因表达。
A cascade of protein phosphorylation, initiated by autophosphorylation of the CheA protein, may be important in the signal transduction pathway of bacterial chemotaxis. A proteolytic fragment of CheA cannot autophosphorylate, but can still transfer phosphate to proteins that generate excitation and adaptation signals. The site of CheA phosphorylation is His 48; mutants altered at this position are non-chemotactic. Similar mechanisms of transient protein phosphorylation and phosphoryl group transfer seem to be involved in processing sensory data and in activating specific gene expression.