Stable assembly of HIV-1 export complexes occurs cotranscriptionally

Isabel Nawroth, Florian Mueller, Eugenia Basyuk, Nancy Beerens, Ulrik Lytt Rahbek, Xavier Darzacq, Edouard Bertrand*, Jørgen Kjems, Ute Schmidt

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review


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
Original languageEnglish
Pages (from-to)1-8
Number of pages8
Publication statusPublished - 1 Jan 2014


  • CRM1
  • HIV-1 Rev
  • Nuclear export


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