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首页> 外文期刊>Biochemistry >Mechanism of Phosphatase Activity in the Chemotaxis Response Regulator CheY
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Mechanism of Phosphatase Activity in the Chemotaxis Response Regulator CheY

机译：趋化反应调节因子CheY中磷酸酶活性的机制

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摘要

Response regulator proteins are phosphorylated on a conserved aspartate to active responses to environmental signals.An intrinsic autophosphatase activity limits the duration of the phosphorylated state.We have previously hypothesized that dephosphorylation might proceed through an intramolecular attack,leading to succinimide formation,and such an intramolecular dephosphorylation event is seen for CheY and OmpR during mass spectrometric analysis [Napper,S.,Wolanin,P.M.,Webre,D.J.,Kindrachuk,J.,Waygood,B., and Stock,J.B.(2003) FEBS Lett 538,77-80].Succinimide formation is usually associated with the spontaneous deamidation of Asn residues.We show here than an Asp 57 to Asn mutant of the CheY chemotaxis response regulator undergoes an unusually rapid deamidation back to the wild-type Asp57,supporting the hypothesis that the active site of CheY is poised for succinimide formation.In contrast,we also show that the major route of phosphoaspartate hydrolysis in CheY occurs through water attack on the phosphorus both during autophosphatase activity and during CheZ-mediated dephosphorylation.Thus,CheY dephosphorylation does not usually proceed via a succinimide or any other intramolecular attack.
机译：反应调节蛋白在保守的天冬氨酸上被磷酸化，从而对环境信号产生主动反应。内在的自磷酸酶活性限制了磷酸化状态的持续时间。我们先前假设去磷酸化可能会通过分子内攻击进行，导致琥珀酰亚胺的形成，以及此类分子内在质谱分析过程中，CheY和OmpR发生了去磷酸化事件[Napper，S.，Wolanin，PM，Webre，DJ，Kindrachuk，J.，Waygood，B。，and Stock，JB（2003）FEBS Lett 538,77-80 ]。琥珀酰亚胺的形成通常与Asn残基的自发脱酰胺作用有关。在此，我们显示了Chey趋化性反应调节剂的Asp 57到Asn突变体经历了异常快速的脱酰胺作用，回到了野生型Asp57，这支持了活性相比之下，我们还表明，CheY中天冬氨酸磷酸酯水解的主要途径是通过水的附着而发生的。在自磷酸酶活性和CheZ介导的去磷酸化过程中都会对磷产生影响。因此，CheY去磷酸化通常不会通过琥珀酰亚胺或任何其他分子内攻击来进行。

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