期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1990
卷号：87
期号：12
页码：4571-4575
DOI：10.1073/pnas.87.12.4571
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
