Trans-activating rev protein of the human immunodeficiency virus 1 interacts directly and specifically with its target RNA.
AUTOR(ES)
Daefler, S
RESUMO
The 20-kDa phosphorylated rev protein from human immunodeficiency virus 1 has been shown to transactivate posttranscriptionally the expression of viral structural proteins by selective stabilization and nuclear export of unspliced and incompletely spliced viral mRNA. We could demonstrate in gel-mobility and immunoprecipitation assays that the recombinant rev protein purified from a baculovirus expression system forms a distinct and specific complex with its target RNA (rev-responsive element), a 234-nucleotide sequence within the envelope coding region of human immunodeficiency virus 1. No complex formation could be observed using RNAs with similar secondary structure nor with other human immunodeficiency virus 1 recombinant proteins. Deletion analysis mapped this specific binding to the first 90 nucleotides of this rev-responsive element, which contains a U2 small nuclear RNA homologous region. We propose that the specific binding of rev to its target RNA sequence plays an essential part in releasing an incompletely spliced viral mRNA containing this target sequence to the cytoplasm.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=54158Documentos Relacionados
- Chemical synthesis of biologically active tat trans-activating protein of human immunodeficiency virus type 1.
- A herpesvirus trans-activating protein interacts with transcription factor OTF-1 and other cellular proteins.
- Subnuclear localization of the trans-activating protein of human T-cell leukemia virus type I.
- Transcriptional trans-activating function of hepatitis B virus.
- Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat.
