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The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP.
Kusters, R; Lentzen, G; Eppens, E; van Geel, A; van der Weijden, C C; Wintermeyer, W; Luirink, J.
Afiliación
  • Kusters R; Department of Molecular Microbiology, Institute of Molecular Biological Sciences, Amsterdam, The Netherlands.
FEBS Lett ; 372(2-3): 253-8, 1995 Sep 25.
Article en En | MEDLINE | ID: mdl-7556679
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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Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Receptores de Péptidos / Receptores Citoplasmáticos y Nucleares / Escherichia coli / Guanosina Trifosfato Idioma: En Revista: FEBS Lett Año: 1995 Tipo del documento: Article País de afiliación: Países Bajos
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Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Receptores de Péptidos / Receptores Citoplasmáticos y Nucleares / Escherichia coli / Guanosina Trifosfato Idioma: En Revista: FEBS Lett Año: 1995 Tipo del documento: Article País de afiliación: Países Bajos