Canova Marc J, Kremer Laurent, Molle Virginie
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.
J Bacteriol. 2009 Apr;191(8):2876-83. doi: 10.1128/JB.01569-08. Epub 2009 Feb 6.
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.
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。