Cotranslational protein targeting in bacteria is mediated by the signal recognition particle (SRP) and FtsY, the bacterial SRP receptor (SR). FtsY is homologous to the SRα subunit of eukaryotes, which is tethered to the membrane via its interaction with the membrane-integral SRβ subunit. Despite the lack of a membrane-anchoring subunit, 30% of FtsY in Escherichia coli are found stably associated with the cytoplasmic membrane. However, the mechanisms that are involved in this membrane association are only poorly understood. Our data indicate that membrane association of FtsY involves two distinct binding sites and that binding to both sites is stabilized by blocking its GTPase activity. Binding to the first site requires only the NG-domain of FtsY and confers protease protection to FtsY. Importantly, the SecY translocon provides the second binding site, to which FtsY binds to form a carbonate-resistant 400-kD FtsY–SecY translocon complex. This interaction is stabilized by the N-terminal A-domain of FtsY, which probably serves as a transient lipid anchor.
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28 August 2006
Article|
August 21 2006
Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
Sandra Angelini,
Sandra Angelini
1Institute for Biochemistry and Molecular Biology, Faculty of Medicine
2Faculty of Biology,
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Diana Boy,
Diana Boy
1Institute for Biochemistry and Molecular Biology, Faculty of Medicine
2Faculty of Biology,
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Emile Schiltz,
Emile Schiltz
3Institute for Organic Chemistry and Biochemistry, University of Freiburg, 79104 Freiburg, Germany
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Hans-Georg Koch
Hans-Georg Koch
1Institute for Biochemistry and Molecular Biology, Faculty of Medicine
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Sandra Angelini
1Institute for Biochemistry and Molecular Biology, Faculty of Medicine
2Faculty of Biology,
Diana Boy
1Institute for Biochemistry and Molecular Biology, Faculty of Medicine
2Faculty of Biology,
Emile Schiltz
3Institute for Organic Chemistry and Biochemistry, University of Freiburg, 79104 Freiburg, Germany
Hans-Georg Koch
1Institute for Biochemistry and Molecular Biology, Faculty of Medicine
Correspondence to Hans-Georg Koch: [email protected]
Abbreviations used in this paper: AMP-PNP, adenyl-5′-yl imidodiphosphate; BN-PAGE, blue native PAGE; GMP-PNP, guanosine 5′-[β,γ-imido] triphosphate; INV, inner membrane vesicle; MtlA, mannitol permease; RNC, ribosome-associated nascent chain; SR, SRP receptor; SRP, signal recognition particle.
Received:
June 20 2006
Accepted:
July 27 2006
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2006
J Cell Biol (2006) 174 (5): 715–724.
Article history
Received:
June 20 2006
Accepted:
July 27 2006
Citation
Sandra Angelini, Diana Boy, Emile Schiltz, Hans-Georg Koch; Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites . J Cell Biol 28 August 2006; 174 (5): 715–724. doi: https://doi.org/10.1083/jcb.200606093
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