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结核分枝杆菌GroEL1伴侣蛋白是丝氨酸/苏氨酸蛋白激酶的底物。

The Mycobacterium tuberculosis GroEL1 chaperone is a substrate of Ser/Thr protein kinases.

作者信息

Canova Marc J, Kremer Laurent, Molle Virginie

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, 69367 Lyon Cedex 07, France.

出版信息

J Bacteriol. 2009 Apr;191(8):2876-83. doi: 10.1128/JB.01569-08. Epub 2009 Feb 6.

DOI:10.1128/JB.01569-08
PMID:19201798
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2668390/
Abstract

We demonstrate that Mycobacterium tuberculosis GroEL1 is phosphorylated by PknF at two positions, Thr25 and Thr54. Unexpectedly, Mycobacterium smegmatis GroEL1 is not a substrate of its cognate PknF. This study shows that the phosphorylation profiles of conserved proteins are species dependent and provide insights that may explain the numerous biological functions of these important proteins.

摘要

我们证明结核分枝杆菌GroEL1在两个位点Thr25和Thr54被PknF磷酸化。出乎意料的是，耻垢分枝杆菌GroEL1不是其同源PknF的底物。这项研究表明保守蛋白的磷酸化谱具有物种依赖性，并提供了可能解释这些重要蛋白众多生物学功能的见解。

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本文引用的文献

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pETPhos: a customized expression vector designed for further characterization of Ser/Thr/Tyr protein kinases and their substrates.pETPhos：一种定制的表达载体，设计用于进一步表征丝氨酸/苏氨酸/酪氨酸蛋白激酶及其底物。
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A Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to induce an inflammatory response in animal models of infection.一种缺乏groEL同源物cpn60.1的结核分枝杆菌突变体是有活力的，但在感染动物模型中未能诱导炎症反应。
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The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates Rv2175c: mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c.结核分枝杆菌丝氨酸/苏氨酸激酶PknL使Rv2175c磷酸化：激活环磷酸化位点的质谱分析及其在Rv2175c募集过程中的作用
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Mycobacterium smegmatis biofilm formation and sliding motility are affected by the serine/threonine protein kinase PknF.耻垢分枝杆菌生物膜形成和滑动运动受丝氨酸/苏氨酸蛋白激酶PknF的影响。
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