ArticleJournal of virology2011
Histone H3 interacts and colocalizes with the nuclear shuttle protein and the movement protein of a geminivirus.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 65 citations in OpenAlex.
- Article
- Article
- Review
- FKBP-type peptidyl-prolyl cis-trans isomerase interacts with the movement protein of tomato leaf curl New Delhi virus and impacts viral replication in Nicotiana benthamiana.Molecular plant pathology · 2022Article
- Insights into the multifunctional roles of geminivirus-encoded proteins in pathogenesis.Archives of virology · 2022Review
- A plant-specific syntaxin-6 protein contributes to the intracytoplasmic route for the begomovirus CabLCV.Plant physiology · 2021Article
- Review
- Genome Editing for Plasmodesmal Biology.Frontiers in plant science · 2021Review
- A single amino acid substitution in the movement protein enables the mechanical transmission of a geminivirus.Molecular plant pathology · 2020Article
- Phosphorylations of the Abutilon Mosaic Virus Movement Protein Affect Its Self-Interaction, Symptom Development, Viral DNA Accumulation, and Host Range.Frontiers in plant science · 2020Article
- A Begomovirus Nuclear Shuttle Protein-Interacting Immune Hub: Hijacking Host Transport Activities and Suppressing Incompatible Functions.Frontiers in plant science · 2020Review
- Dynamic Subcellular Localization, Accumulation, and Interactions of Proteins FromFrontiers in plant science · 2020Article
- Characterization of Curtovirus V2 Protein, a Functional Homolog of Begomovirus V2.Frontiers in plant science · 2020Article
- Multifaceted role of geminivirus associated betasatellite in pathogenesis.Molecular plant pathology · 2019Review
- Plant Antiviral Immunity Against Geminiviruses and Viral Counter-Defense for Survival.Frontiers in microbiology · 2019Review
- Begomoviral Movement Protein Effects in Human and Plant Cells: Towards New Potential Interaction Partners.Viruses · 2017Article
- The replication initiator protein of a geminivirus interacts with host monoubiquitination machinery and stimulates transcription of the viral genome.PLoS pathogens · 2017Article
- Analyses of pea necrotic yellow dwarf virus-encoded proteins.Virus genes · 2017Article
- The Nucleolar Fibrillarin Protein Is Required for Helper Virus-Independent Long-Distance Trafficking of a Subviral Satellite RNA in Plants.The Plant cell · 2016Article
- Two Populations of Viral Minichromosomes Are Present in a Geminivirus-Infected Plant Showing Symptom Remission (Recovery).Journal of virology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Geminiviruses are plant-infecting viruses with small circular single-stranded DNA genomes. These viruses utilize nuclear shuttle proteins (NSPs) and movement proteins (MPs) for trafficking of infectious DNA through the nuclear pore complex and plasmodesmata, respectively. Here, a biochemical approach was used to identify host factors interacting with the NSP and MP of the geminivirus Bean dwarf mosaic virus (BDMV). Based on these studies, we identified and characterized a host nucleoprotein, histone H3, which interacts with both the NSP and MP. The specific nature of the interaction of histone H3 with these viral proteins was established by gel overlay and in vitro and in vivo coimmunoprecipitation (co-IP) assays. The NSP and MP interaction domains were mapped to the N-terminal region of histone H3. These experiments also revealed a direct interaction between the BDMV NSP and MP, as well as interactions between histone H3 and the capsid proteins of various geminiviruses. Transient-expression assays revealed the colocalization of histone H3 and NSP in the nucleus and nucleolus and of histone H3 and MP in the cell periphery and plasmodesmata. Finally, using in vivo co-IP assays with a Myc-tagged histone H3, a complex composed of histone H3, NSP, MP, and viral DNA was recovered. Taken together, these findings implicate the host factor histone H3 in the process by which an infectious geminiviral DNA complex forms within the nucleus for export to the cell periphery and cell-to-cell movement through plasmodesmata.
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