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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...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2006
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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. |
format | Text |
id | pubmed-2064314 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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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