ArticleRetrovirology2017
Modulation of the functional association between the HIV-1 intasome and the nucleosome by histone amino-terminal tails.
Article in Retrovirology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Molecular basis for the regulation of retroviral nucleosomal integration by chromatin compaction.Nucleic acids research · 2026Article
- Aquarius helicase facilitates HIV-1 integration into R-loop enriched genomic regions.Nature microbiology · 2025Article
- Temporal and spatial niche partitioning in a retrotransposon community of the Drosophila melanogaster genome.Nucleic acids research · 2025Article
- Modulation of the functional interfaces between retroviral intasomes and the human nucleosome.mBio · 2023Article
- Review
- HIV-1 Preintegration Complex Preferentially Integrates the Viral DNA into Nucleosomes Containing Trimethylated Histone 3-Lysine 36 Modification and Flanking Linker DNA.Journal of virology · 2022Article
- Review
- Review
- Modulation of the intrinsic chromatin binding property of HIV-1 integrase by LEDGF/p75.Nucleic acids research · 2021Article
- Factors that mold the nuclear landscape of HIV-1 integration.Nucleic acids research · 2021Review
- Targeting Epigenetics to Cure HIV-1: Lessons From (and for) Cancer Treatment.Frontiers in cellular and infection microbiology · 2021Review
- The chromatin landscape at the HIV-1 provirus integration site determines viral expression.Nucleic acids research · 2020Article
- Review
- Human H4 tail stimulates HIV-1 integration through binding to the carboxy-terminal domain of integrase.Nucleic acids research · 2019Article
- Impact of LEDGIN treatment during virus production on residual HIV-1 transcription.Retrovirology · 2019Article
Corrections and comments
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Authors and funding
20 authors at 5 institutions in 3 countries.
Funding
Abstract
backgroundStable insertion of the retroviral DNA genome into host chromatin requires the functional association between the intasome (integrase·viral DNA complex) and the nucleosome. The data from the literature suggest that direct protein-protein contacts between integrase and histones may be involved in anchoring the intasome to the nucleosome. Since histone tails are candidates for interactions with the incoming intasomes we have investigated whether they could participate in modulating the nucleosomal integration process.
resultsWe show here that histone tails are required for an optimal association between HIV-1 integrase (IN) and the nucleosome for efficient integration. We also demonstrate direct interactions between IN and the amino-terminal tail of human histone H4 in vitro. Structure/function studies enabled us to identify amino acids in the carboxy-terminal domain of IN that are important for this interaction. Analysis of the nucleosome-binding properties of catalytically active mutated INs confirmed that their ability to engage the nucleosome for integration in vitro was affected. Pseudovirus particles bearing mutations that affect the IN/H4 association also showed impaired replication capacity due to altered integration and re-targeting of their insertion sites toward dynamic regions of the chromatin with lower nucleosome occupancy.
conclusionsCollectively, our data support a functional association between HIV-1 IN and histone tails that promotes anchoring of the intasome to nucleosomes and optimal integration into chromatin.
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