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

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...

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Autores principales: Angelini, Sandra, Boy, Diana, Schiltz, Emile, Koch, Hans-Georg
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064314/
https://www.ncbi.nlm.nih.gov/pubmed/16923832
http://dx.doi.org/10.1083/jcb.200606093
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author Angelini, Sandra
Boy, Diana
Schiltz, Emile
Koch, Hans-Georg
author_facet Angelini, Sandra
Boy, Diana
Schiltz, Emile
Koch, Hans-Georg
author_sort Angelini, Sandra
collection PubMed
description 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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spelling pubmed-20643142007-11-29 Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites Angelini, Sandra Boy, Diana Schiltz, Emile Koch, Hans-Georg J Cell Biol Research Articles 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. The Rockefeller University Press 2006-08-28 /pmc/articles/PMC2064314/ /pubmed/16923832 http://dx.doi.org/10.1083/jcb.200606093 Text en Copyright © 2006, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Angelini, Sandra
Boy, Diana
Schiltz, Emile
Koch, Hans-Georg
Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
title Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
title_full Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
title_fullStr Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
title_full_unstemmed Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
title_short Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
title_sort membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064314/
https://www.ncbi.nlm.nih.gov/pubmed/16923832
http://dx.doi.org/10.1083/jcb.200606093
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