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Published online 21 August 2006. doi:10.1083/jcb.200606093
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 5, 715-724
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Article

Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites



Sandra Angelini1,2, Diana Boy1,2, Emile Schiltz3, and Hans-Georg Koch1

1 Institute for Biochemistry and Molecular Biology, Faculty of Medicine, 2 Faculty of Biology, and 3 Institute for Organic Chemistry and Biochemistry, University of Freiburg, 79104 Freiburg, Germany

Correspondence to Hans-Georg Koch: Hans-Georg.Koch{at}biochemie.uni-freiburg.de

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 SR{alpha} subunit of eukaryotes, which is tethered to the membrane via its interaction with the membrane-integral SRß 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.

Abbreviations used in this paper: AMP-PNP, adenyl-5'-yl imidodiphosphate; BN-PAGE, blue native PAGE; GMP-PNP, guanosine 5'-[ß,{gamma}-imido] triphosphate; INV, inner membrane vesicle; MtlA, mannitol permease; RNC, ribosome-associated nascent chain; SR, SRP receptor; SRP, signal recognition particle.


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