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

    Research output: Contribution to journalArticleAcademicpeer-review

    40 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 languageEnglish
    Pages (from-to)253-258
    Number of pages6
    JournalFEBS letters
    Volume372
    Issue number2-3
    DOIs
    Publication statusPublished - 25 Sep 1995

    Fingerprint

    Protein Transport
    Guanosine Triphosphate
    Escherichia coli
    Proteins
    Signal Recognition Particle
    GTP Phosphohydrolases
    Mutant Proteins
    GTP-Binding Proteins
    Hydrolysis
    Peptide Hydrolases
    signal peptide receptor

    Keywords

    • Escherichia coli
    • FtsY
    • Protein-targeting
    • Signal recognition particle

    Cite this

    Kusters, Ron ; Lentzen, Georg ; Eppens, Elaine ; van Geel, Anton ; van der Weijden, Coen C. ; Wintermeyer, Wolfgang ; Luirink, Joen. / The functioning of the SRP receptor FtsY in protein-targeting in E. coli is correlated with its ability to bind and hydrolyse GTP. In: FEBS letters. 1995 ; Vol. 372, No. 2-3. pp. 253-258.
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    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.",
    keywords = "Escherichia coli, FtsY, Protein-targeting, Signal recognition particle",
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    year = "1995",
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    Kusters, R, Lentzen, G, Eppens, E, van Geel, A, van der Weijden, CC, Wintermeyer, W & 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 letters, vol. 372, no. 2-3, pp. 253-258. https://doi.org/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. / Kusters, Ron; Lentzen, Georg; Eppens, Elaine; van Geel, Anton; van der Weijden, Coen C.; Wintermeyer, Wolfgang; Luirink, Joen.

    In: FEBS letters, Vol. 372, No. 2-3, 25.09.1995, p. 253-258.

    Research output: Contribution to journalArticleAcademicpeer-review

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