PMID:7556679

Citation	Kusters, R, Lentzen, G, Eppens, E, van Geel, A, van der Weijden, CC, Wintermeyer, W and Luirink, J (1995) The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP. FEBS Lett. 372:253-8
Abstract	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.
Links	PubMed
Keywords	Base Sequence; Escherichia coli/genetics; Escherichia coli/metabolism; GTP-Binding Proteins/metabolism; Guanosine Triphosphate/metabolism; Hydrolysis; Molecular Sequence Data; Mutagenesis, Site-Directed; Receptors, Cytoplasmic and Nuclear/genetics; Receptors, Cytoplasmic and Nuclear/metabolism; Receptors, Peptide/genetics; Receptors, Peptide/metabolism
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