Cargando…
TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins
Twin-arginine-containing signal sequences mediate the transmembrane transport of folded proteins. The cognate twin-arginine translocation (Tat) machinery of Escherichia coli consists of the membrane proteins TatA, TatB, and TatC. Whereas Tat signal peptides are recognized by TatB and TatC, little is...
Autores principales: | , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2993744/ https://www.ncbi.nlm.nih.gov/pubmed/20926683 http://dx.doi.org/10.1091/mbc.E10-07-0585 |
_version_ | 1782192843144560640 |
---|---|
author | Maurer, Carlo Panahandeh, Sascha Jungkamp, Anna-Carina Moser, Michael Müller, Matthias |
author_facet | Maurer, Carlo Panahandeh, Sascha Jungkamp, Anna-Carina Moser, Michael Müller, Matthias |
author_sort | Maurer, Carlo |
collection | PubMed |
description | Twin-arginine-containing signal sequences mediate the transmembrane transport of folded proteins. The cognate twin-arginine translocation (Tat) machinery of Escherichia coli consists of the membrane proteins TatA, TatB, and TatC. Whereas Tat signal peptides are recognized by TatB and TatC, little is known about molecular contacts of the mature, folded part of Tat precursor proteins. We have placed a photo-cross-linker into Tat substrates at sites predicted to be either surface-exposed or hidden in the core of the folded proteins. On targeting of these variants to the Tat machinery of membrane vesicles, all surface-exposed sites were found in close proximity to TatB. Correspondingly, incorporation of the cross-linker into TatB revealed multiple precursor-binding sites in the predicted transmembrane and amphipathic helices of TatB. Large adducts indicative of TatB oligomers contacting one precursor molecule were also obtained. Cross-linking of Tat substrates to TatB required an intact twin-arginine signal peptide and disappeared upon transmembrane translocation. Our collective data are consistent with TatB forming an oligomeric binding site that transiently accommodates folded Tat precursors. |
format | Text |
id | pubmed-2993744 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-29937442011-02-16 TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins Maurer, Carlo Panahandeh, Sascha Jungkamp, Anna-Carina Moser, Michael Müller, Matthias Mol Biol Cell Articles Twin-arginine-containing signal sequences mediate the transmembrane transport of folded proteins. The cognate twin-arginine translocation (Tat) machinery of Escherichia coli consists of the membrane proteins TatA, TatB, and TatC. Whereas Tat signal peptides are recognized by TatB and TatC, little is known about molecular contacts of the mature, folded part of Tat precursor proteins. We have placed a photo-cross-linker into Tat substrates at sites predicted to be either surface-exposed or hidden in the core of the folded proteins. On targeting of these variants to the Tat machinery of membrane vesicles, all surface-exposed sites were found in close proximity to TatB. Correspondingly, incorporation of the cross-linker into TatB revealed multiple precursor-binding sites in the predicted transmembrane and amphipathic helices of TatB. Large adducts indicative of TatB oligomers contacting one precursor molecule were also obtained. Cross-linking of Tat substrates to TatB required an intact twin-arginine signal peptide and disappeared upon transmembrane translocation. Our collective data are consistent with TatB forming an oligomeric binding site that transiently accommodates folded Tat precursors. The American Society for Cell Biology 2010-12-01 /pmc/articles/PMC2993744/ /pubmed/20926683 http://dx.doi.org/10.1091/mbc.E10-07-0585 Text en © 2010 by The American Society for Cell Biology This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial –Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). |
spellingShingle | Articles Maurer, Carlo Panahandeh, Sascha Jungkamp, Anna-Carina Moser, Michael Müller, Matthias TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins |
title | TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins |
title_full | TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins |
title_fullStr | TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins |
title_full_unstemmed | TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins |
title_short | TatB Functions as an Oligomeric Binding Site for Folded Tat Precursor Proteins |
title_sort | tatb functions as an oligomeric binding site for folded tat precursor proteins |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2993744/ https://www.ncbi.nlm.nih.gov/pubmed/20926683 http://dx.doi.org/10.1091/mbc.E10-07-0585 |
work_keys_str_mv | AT maurercarlo tatbfunctionsasanoligomericbindingsiteforfoldedtatprecursorproteins AT panahandehsascha tatbfunctionsasanoligomericbindingsiteforfoldedtatprecursorproteins AT jungkampannacarina tatbfunctionsasanoligomericbindingsiteforfoldedtatprecursorproteins AT mosermichael tatbfunctionsasanoligomericbindingsiteforfoldedtatprecursorproteins AT mullermatthias tatbfunctionsasanoligomericbindingsiteforfoldedtatprecursorproteins |