The First HxRxG Motif in Simian Immunodeficiency Virus mac239 Vpr Is Crucial for G 2 /M Cell Cycle Arrest
Open Access
- 15 November 2002
- journal article
- research article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 76 (22) , 11704-11709
- https://doi.org/10.1128/jvi.76.22.11704-11709.2002
Abstract
The highly conserved Vpr protein mediates cell cycle arrest, transcriptional transactivation, and nuclear import of the preintegration complex in human immunodeficiency virus type 1. To identify functional domains in simian immunodeficiency virus (SIV) mac239 Vpr, we mutagenized selected motifs within an α-helical region and two C-terminal HxRxG motifs. All Vpr mutants located to the nucleus. Substitution of four amino acids in the α-helical domain did not interfere with cell cycle arrest, while a single substitution abolished cell cycle arrest function. Mutation of the first HxRxG motif to AxAxA also resulted in loss of cell cycle arrest, while mutation of the second motif had no effect. Interestingly, both Vpr mutants impaired in cell cycle arrest function also showed reduced transactivation of the SIV long terminal repeat, suggesting that arrest of cells at G 2 /M mediates or contributes to transactivation by Vpr.Keywords
This publication has 18 references indexed in Scilit:
- Human Immunodeficiency Virus Type 1 Vpr Induces Apoptosis in Human Neuronal CellsJournal of Virology, 2000
- Induction of Apoptosis by the Vpr Protein of Human Immunodeficiency Virus Type 1 Occurs Independently of G2 Arrest of the Cell CycleVirology, 2000
- Residues within the HFRIGC Sequence of HIV-1 Vpr Involved in Growth Arrest ActivitiesBiochemical and Biophysical Research Communications, 1999
- Human immunodeficiency virus type 1 vpr protein transactivation function: mechanism and identification of domains involvedJournal of Molecular Biology, 1998
- Human immunodeficiency virus type 1 Vpr localization: nuclear transport of a viral protein modulated by a putative amphipathic helical structure and its relevance to biological activityJournal of Molecular Biology, 1998
- Mutagenesis of the putative alpha-helical domain of the Vpr protein of human immunodeficiency virus type 1: effect on stability and virion incorporation.Proceedings of the National Academy of Sciences, 1995
- A domain of human immunodeficiency virus type 1 Vpr containing repeated H(S/F)RIG amino acid motifs causes cell growth arrest and structural defects.Proceedings of the National Academy of Sciences, 1995
- Epitope-tag vectors for eukaryotic protein productionGene, 1995
- The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells.Proceedings of the National Academy of Sciences, 1994
- Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure.Proceedings of the National Academy of Sciences, 1987