金黄色葡萄球菌自诱导物-2 合酶 LuxS 通过丝氨酸/苏氨酸磷酸化调节。
The Staphylococcus aureus autoinducer-2 synthase LuxS is regulated by Ser/Thr phosphorylation.
机构信息
Institut de Biologie et Chimie des Protéines (IBCP UMR 5086), CNRS, Université Lyon 1, IFR128 BioSciences, Lyon-Gerland, 7 Passage du Vercors, Lyon Cedex 07, France.
出版信息
J Bacteriol. 2010 Dec;192(23):6295-301. doi: 10.1128/JB.00853-10. Epub 2010 Sep 24.
Abstract
The Staphylococcus aureus autoinducer-2 (AI-2) producer protein LuxS is phosphorylated by the Ser/Thr kinase Stk1 at a unique position, Thr14. The enzymatic activity of the phosphorylated isoform of LuxS was abrogated compared to that of nonphosphorylated LuxS, thus providing the first evidence of an AI-2-producing enzyme regulated by phosphorylation and demonstrating that S. aureus possesses an original and specific system for controlling AI-2 synthesis.
摘要
金黄色葡萄球菌自诱导物-2（AI-2）产生蛋白 LuxS 在一个独特的位置 Thr14 被 Ser/Thr 激酶 Stk1 磷酸化。与非磷酸化 LuxS 相比，磷酸化同工型的 LuxS 的酶活性被阻断，从而首次提供了一种 AI-2 产生酶受磷酸化调节的证据，并证明金黄色葡萄球菌拥有一种原始而特异的系统来控制 AI-2 的合成。
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