The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP

Ron Kusters; Georg Lentzen; Elaine Eppens; Anton van Geel; Coen C. van der Weijden; Wolfgang Wintermeyer; Joen Luirink

doi:10.1016/0014-5793(95)00997-N

The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP

Ron Kusters, Georg Lentzen, Elaine Eppens, Anton van Geel, Coen C. van der Weijden, Wolfgang Wintermeyer, Joen Luirink^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

42 Citations (Scopus)

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.

Original language	English
Pages (from-to)	253-258
Number of pages	6
Journal	FEBS letters
Volume	372
Issue number	2-3
DOIs	https://doi.org/10.1016/0014-5793(95)00997-N
Publication status	Published - 25 Sept 1995
Externally published	Yes

Keywords

Escherichia coli
FtsY
Protein-targeting
Signal recognition particle

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10.1016/0014-5793(95)00997-N

Cite this

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title = "The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP",

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.",

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doi = "10.1016/0014-5793(95)00997-N",

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T1 - The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP

AU - Kusters, Ron

AU - Lentzen, Georg

AU - Eppens, Elaine

AU - van Geel, Anton

AU - van der Weijden, Coen C.

AU - Wintermeyer, Wolfgang

AU - Luirink, Joen

PY - 1995/9/25

Y1 - 1995/9/25

N2 - 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.

AB - 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.

KW - Escherichia coli

KW - FtsY

KW - Protein-targeting

KW - Signal recognition particle

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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

Abstract

Keywords

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