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Stable assembly of HIV-1 export complexes occurs cotranscriptionally
The HIV-1 Rev protein mediates export of unspliced and singly spliced viral transcripts by binding to the Rev response element (RRE) and recruiting the cellular export factor CRM1. Here, we investigated the recruitment of Rev to the transcription sites of HIV-1 reporters that splice either post- or...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3866638/ https://www.ncbi.nlm.nih.gov/pubmed/24255166 http://dx.doi.org/10.1261/rna.038182.113 |
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author | Nawroth, Isabel Mueller, Florian Basyuk, Eugenia Beerens, Nancy Rahbek, Ulrik L. Darzacq, Xavier Bertrand, Edouard Kjems, Jørgen Schmidt, Ute |
author_facet | Nawroth, Isabel Mueller, Florian Basyuk, Eugenia Beerens, Nancy Rahbek, Ulrik L. Darzacq, Xavier Bertrand, Edouard Kjems, Jørgen Schmidt, Ute |
author_sort | Nawroth, Isabel |
collection | PubMed |
description | The HIV-1 Rev protein mediates export of unspliced and singly spliced viral transcripts by binding to the Rev response element (RRE) and recruiting the cellular export factor CRM1. Here, we investigated the recruitment of Rev to the transcription sites of HIV-1 reporters that splice either post- or cotranscriptionally. In both cases, we observed that Rev localized to the transcription sites of the reporters and recruited CRM1. Rev and CRM1 remained at the reporter transcription sites when cells were treated with the splicing inhibitor Spliceostatin A (SSA), showing that the proteins associate with RNA prior to or during early spliceosome assembly. Fluorescence recovery after photobleaching (FRAP) revealed that Rev and CRM1 have similar kinetics as the HIV-1 RNA, indicating that Rev, CRM1, and RRE-containing RNAs are released from the site of transcription in one single export complex. These results suggest that cotranscriptional formation of a stable export complex serves as a means to ensure efficient export of unspliced viral RNAs. |
format | Online Article Text |
id | pubmed-3866638 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-38666382015-01-01 Stable assembly of HIV-1 export complexes occurs cotranscriptionally Nawroth, Isabel Mueller, Florian Basyuk, Eugenia Beerens, Nancy Rahbek, Ulrik L. Darzacq, Xavier Bertrand, Edouard Kjems, Jørgen Schmidt, Ute RNA Articles The HIV-1 Rev protein mediates export of unspliced and singly spliced viral transcripts by binding to the Rev response element (RRE) and recruiting the cellular export factor CRM1. Here, we investigated the recruitment of Rev to the transcription sites of HIV-1 reporters that splice either post- or cotranscriptionally. In both cases, we observed that Rev localized to the transcription sites of the reporters and recruited CRM1. Rev and CRM1 remained at the reporter transcription sites when cells were treated with the splicing inhibitor Spliceostatin A (SSA), showing that the proteins associate with RNA prior to or during early spliceosome assembly. Fluorescence recovery after photobleaching (FRAP) revealed that Rev and CRM1 have similar kinetics as the HIV-1 RNA, indicating that Rev, CRM1, and RRE-containing RNAs are released from the site of transcription in one single export complex. These results suggest that cotranscriptional formation of a stable export complex serves as a means to ensure efficient export of unspliced viral RNAs. Cold Spring Harbor Laboratory Press 2014-01 /pmc/articles/PMC3866638/ /pubmed/24255166 http://dx.doi.org/10.1261/rna.038182.113 Text en © 2013 Nawroth et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/3.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/. |
spellingShingle | Articles Nawroth, Isabel Mueller, Florian Basyuk, Eugenia Beerens, Nancy Rahbek, Ulrik L. Darzacq, Xavier Bertrand, Edouard Kjems, Jørgen Schmidt, Ute Stable assembly of HIV-1 export complexes occurs cotranscriptionally |
title | Stable assembly of HIV-1 export complexes occurs cotranscriptionally |
title_full | Stable assembly of HIV-1 export complexes occurs cotranscriptionally |
title_fullStr | Stable assembly of HIV-1 export complexes occurs cotranscriptionally |
title_full_unstemmed | Stable assembly of HIV-1 export complexes occurs cotranscriptionally |
title_short | Stable assembly of HIV-1 export complexes occurs cotranscriptionally |
title_sort | stable assembly of hiv-1 export complexes occurs cotranscriptionally |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3866638/ https://www.ncbi.nlm.nih.gov/pubmed/24255166 http://dx.doi.org/10.1261/rna.038182.113 |
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