Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains

被引：72
|
作者：
Grundner, C [1 ]
Gay, LM [1 ]
Alber, T [1 ]
机构：
[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
来源：
PROTEIN SCIENCE | 2005年 / 14卷 / 07期
关键词：
FHA domain; protein phosphorylation; serine/threonine protein kinase; signaling;
D O I：
10.1110/ps.051413405
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The physiologic roles and the substrates of the Mycobacterium tuberculosis (Mtb) serine/threonine kinases are largely unknown. Here, we report six novel interactions of PknB, PknD, PknE, and PknF with the Forkhead-Associated (FHA) domains of Rv0020c and the putative ABC transporter Rv1747. Purified PknB and PknF kinase domains phosphorylated multiple FHA-domain proteins in vitro. Although they remain to be verified in vivo, these reactions suggest a web of interactions between STPKs and FHA domains.
引用
收藏
页码：1918 / 1921
页数：4
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