ArticleNucleic acids research2011
The in vitro loose dimer structure and rearrangements of the HIV-2 leader RNA.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 28 citations in OpenAlex.
- Dissection of the EIAV Core Packaging Region Identifies SL2 Stem and SL2-SL3 Junction as Gag-Associated Packaging Determinants and Antiviral Targets.International journal of molecular sciences · 2026Article
- Elements in the 5' Untranslated Region of Viral RNA Important for HIV Gag Recognition and Cross-Packaging.Viruses · 2025Article
- Mapping the structural landscape of the yeast Ty3 retrotransposon RNA genome.Nucleic acids research · 2024Article
- Human Retrovirus Genomic RNA Packaging.Viruses · 2022Review
- Highly conserved s2m element of SARS-CoV-2 dimerizes via a kissing complex and interacts with host miRNA-1307-3p.Nucleic acids research · 2022Article
- Specific Guanosines in the HIV-2 Leader RNA are Essential for Efficient Viral Genome Packaging.Journal of molecular biology · 2021Article
- Retroviral-like determinants and functions required for dimerization of Ty1 retrotransposon RNA.RNA biology · 2019Article
- New windows into retroviral RNA structures.Retrovirology · 2018Review
- Retroviral RNA Dimerization: From Structure to Functions.Frontiers in microbiology · 2018Review
- A normal genetic variation modulates synaptic MMP-9 protein levels and the severity of schizophrenia symptoms.EMBO molecular medicine · 2017Article
- Article
- Determinants of Genomic RNA Encapsidation in the Saccharomyces cerevisiae Long Terminal Repeat Retrotransposons Ty1 and Ty3.Viruses · 2016Review
- The matrix domain contributes to the nucleic acid chaperone activity of HIV-2 Gag.Retrovirology · 2016Article
- Conserved determinants of lentiviral genome dimerization.Retrovirology · 2015Article
- Ty1 retrovirus-like element Gag contains overlapping restriction factor and nucleic acid chaperone functions.Nucleic acids research · 2015Article
- Similarities and differences in the nucleic acid chaperone activity of HIV-2 and HIV-1 nucleocapsid proteins in vitro.Retrovirology · 2014Article
- Influence of RNA structural elements on Ty1 retrotransposition.Mobile genetic elements · 2013Article
- Comparison of SIV and HIV-1 genomic RNA structures reveals impact of sequence evolution on conserved and non-conserved structural motifs.PLoS pathogens · 2013Article
- Automated 3D structure composition for large RNAs.Nucleic acids research · 2012Article
- Different effects of the TAR structure on HIV-1 and HIV-2 genomic RNA translation.Nucleic acids research · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA dimerization is an essential step in the retroviral life cycle. Dimerization and encapsidation signals, closely linked in HIV-2, are located in the leader RNA region. The SL1 motif and nucleocapsid protein are considered important for both processes. In this study, we show the structure of the HIV-2 leader RNA (+1-560) captured as a loose dimer. Potential structural rearrangements within the leader RNA were studied. In the loose dimer form, the HIV-2 leader RNA strand exists in vitro as a single global fold. Two kissing loop interfaces within the loose dimer were identified: SL1/SL1 and TAR/TAR. Evidence for these findings is provided by RNA probing using SHAPE, chemical reagents, enzymes, non-denaturing PAGE mobility assays, antisense oligonucleotides hybridization and analysis of an RNA mutant. Both TAR and SL1 as isolated domains are bound by recombinant NCp8 protein with high affinity, contrary to the hairpins downstream of SL1. Foot-printing of the SL1/NCp8 complex indicates that the major binding site maps to the SL1 upper stem. Taken together, these data suggest a model in which TAR hairpin III, the segment of SL1 proximal to the loop and the PAL palindromic sequence play specific roles in the initiation of dimerization.
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