Phosphoaspartates in bacterial signal transduction
Phosphoaspartates in bacterial signal transduction
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DOI：
10.1016/s0959-440x(01)00271-8
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发表时间：
2001-12-01
影响因子：
6.8
通讯作者：
Wemmer, DE
中科院分区：
文献类型：
--
作者：
Cho, HS;Pelton, JG;Wemmer, DE
细菌使用称为双组分信号转导的策略来感知各种刺激并启动适当的反应。信号处理开始于被称为组氨酸激酶的蛋白质。在大多数情况下，这些是对环境线索做出反应的膜结合受体。组氨酸激酶使用ATP作为磷酸供体来磷酸化保守的组氨酸残基。随后将磷酰基转移到同源反应调节剂中的保守的N-乙酰基残基导致适当的输出。最近的结构研究激活（磷酸化）的反应调节剂和它们的磷酸盐轴承调节结构域提供了深入了解这些无处不在的调节蛋白的化学和生物学之间的联系。其功能的化学方面似乎广泛地概括为采用磷酸天冬氨酸中间体的酶。
Bacteria use a strategy referred to as two-component signal transduction to sense a variety of stimuli and initiate an appropriate response. Signal processing begins with proteins referred to as histidine kinases. In most cases, these are membrane-bound receptors that respond to environmental cues. Histidine kinases use ATP as a phosphodonor to phosphorylate a conserved histidine residue. Subsequent transfer of the phosphoryl group to a conserved aspartyl residue in the cognate response regulator results in an appropriate output. Recent structural studies of activated (phosphorylated) response regulators and their aspartate-bearing regulatory domains have provided insight into the links between the chemistry and biology of these ubiquitous regulatory proteins. Chemical aspects of their function appear to generalize broadly to enzymes that adopt a phosphoaspartate intermediate.