An ancient family of human endogenous retroviruses encodes a functional homolog of the HIV-1 Rev protein
- 9 November 1999
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 96 (23) , 13404-13408
- https://doi.org/10.1073/pnas.96.23.13404
Abstract
The human endogenous retrovirus K (HERV-K) family of endogenous retroviruses consists of ≈50 proviral copies per haploid human genome. Herein, the HERV-Ks are shown to encode a sequence-specific nuclear RNA export factor, termed K-Rev, that is functionally analogous to the HIV-1 Rev protein. Like HIV-1 Rev, K-Rev binds to both the Crm1 nuclear export factor and to a cis-acting viral RNA target to activate nuclear export of unspliced RNAs. Surprisingly, this HERV-K RNA sequence, which is encoded within the HERV-K long terminal repeat, is also recognized by HIV-1 Rev. These data provide surprising evidence for an evolutionary link between HIV-1 and a group of endogenous retroviruses that first entered the human genome ≈30 million years ago.Keywords
This publication has 53 references indexed in Scilit:
- THE HIV-1 REV PROTEINAnnual Review of Microbiology, 1998
- Retroviruses as Model Systems for the Study of Nuclear RNA Export PathwaysVirology, 1998
- Our retroviral heritageTrends in Genetics, 1997
- The viruses in all of us: characteristics and biological significance of human endogenous retrovirus sequences.Proceedings of the National Academy of Sciences, 1996
- RanGAP1 induces GTPase activity of nuclear Ras-related Ran.Proceedings of the National Academy of Sciences, 1994
- Identification of human endogenous retroviruses with complex mRNA expression and particle formation.Proceedings of the National Academy of Sciences, 1993
- The HIV-1 Tat protein activates transcription from an upstream DNA-binding site: implications for Tat function.Genes & Development, 1991
- Oligomerization and RNA binding domains of the type 1 human immunodeficiency virus Rev protein: a dual function for an arginine-rich binding motif.Proceedings of the National Academy of Sciences, 1991
- HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: Implications for HIV-1 latencyCell, 1991
- Functional dissection of the HIV-1 Rev trans-activator—Derivation of a trans-dominant repressor of Rev functionCell, 1989