THE FUNCTIONING OF THE SRP RECEPTOR FTSY IN PROTEIN-TARGETING IN ESCHERICHIA-COLI CORRELATED WITH ITS ABILITY TO BIND AND HYDROLYZE GTP

被引：45
作者：
KUSTERS, R
LENTZEN, G
EPPENS, E
VANGEEL, A
VANDERWEIJDEN, CC
WINTERMEYER, W
LUIRINK, J
机构：
[1] INST MOLEC BIOL SCI,DEPT MOLEC MICROBIOL,1081 HV AMSTERDAM,NETHERLANDS
[2] INST MOLEC BIOL SCI,DEPT MOLEC MICROBIOL,1081 HV AMSTERDAM,NETHERLANDS
来源：
FEBS LETTERS | 1995年 / 372卷 / 2-3期
关键词：
ESCHERICHIA COLI; FTSY; PROTEIN-TARGETING; SIGNAL RECOGNITION PARTICLE;
D O I：
10.1016/0014-5793(95)00997-N
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：
In this study, we have established that FtsY, the E. coli homolog of the mammalian signal recognition particle (SRP) receptor, is a GTP-binding protein which displays intrinsic GTPase activity. GTP was found to influence the protease sensitivity of FtsY indicative of a conformational change. FtsY mutated in the 4th GTP-binding consensus element displayed reduced GTP-binding and -hydrolysis which correlated with a reduced ability to interact with SRP. Overexpression of the mutant proteins had a stronger inhibitory effect on protein translocation than overexpression of wild-type FtsY. These observations suggest that in E. coli GTP is important for proper functioning of FtsY in protein-targeting.
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页码：253 / 258
页数：6
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