The Mycobacterium tuberculosis GroEL1 Chaperone Is a Substrate of Ser/Thr Protein Kinases

被引：41
作者：
Canova, Marc J. [1 ]
Kremer, Laurent [1 ,2 ,3 ,4 ]
Molle, Virginie [1 ]
机构：
[1] Univ Lyon 1, IBCP UMR 5086, CNRS, IFR128 BioSci,Inst Biol & Chim Prot, F-69367 Lyon 07, France
[2] Univ Montpellier 2, Lab Dynam Interact Membranaires Normales & Pathol, F-34095 Montpellier 05, France
[3] Univ Montpellier 1, CNRS 5235, F-34095 Montpellier 05, France
[4] DIMNP, INSERM, F-34095 Montpellier 05, France
来源：
JOURNAL OF BACTERIOLOGY | 2009年 / 191卷 / 08期
关键词：
MYCOLIC ACID BIOSYNTHESIS; SERINE/THREONINE KINASE; BIOFILM FORMATION; ESCHERICHIA-COLI; ABC TRANSPORTER; FHA DOMAINS; PHOSPHORYLATION; PKNF; INFECTION; EXPRESSION;
D O I：
10.1128/JB.01569-08
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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.
引用
收藏
页码：2876 / 2883
页数：8
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