ArticleNature structural & molecular biology2014
Ty3 reverse transcriptase complexed with an RNA-DNA hybrid shows structural and functional asymmetry.
Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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
20 citing papers in PubMed.
- Origin and Evolution of Plant Long Terminal Repeat Retrotransposons with Additional Ribonuclease H.Genome biology and evolution · 2023Article
- Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.Nature structural & molecular biology · 2023Review
- Human endogenous retrovirus-K (HERV-K) reverse transcriptase (RT) structure and biochemistry reveals remarkable similarities to HIV-1 RT and opportunities for HERV-K-specific inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis of Ty3 retrotransposon integration at RNA Polymerase III-transcribed genes.Nature communications · 2021Article
- Structures of Substrate Complexes of Foamy Viral Protease-Reverse Transcriptase.Journal of virology · 2021Article
- Crystal Structure of a Retroviral Polyprotein: Prototype Foamy Virus Protease-Reverse Transcriptase (PR-RT).Viruses · 2021Article
- Retroviral RNase H: Structure, mechanism, and inhibition.The Enzymes · 2021Review
- Review
- Convergent evolution of integration site selection upstream of tRNA genes by yeast and amoeba retrotransposons.Nucleic acids research · 2018Article
- Multiple Partial Regularized Nonnegative Matrix Factorization for Predicting Ontological Functions of lncRNAs.Frontiers in genetics · 2018Article
- Specific reverse transcriptase slippage at the HIV ribosomal frameshift sequence: potential implications for modulation of GagPol synthesis.Nucleic acids research · 2017Article
- Characterization of Echinostoma cinetorchis endoribonuclease, RNase H.The Korean journal of parasitology · 2017Article
- Arm-specific cleavage and mutation during reverse transcription of 2΄,5΄-branched RNA by Moloney murine leukemia virus reverse transcriptase.Nucleic acids research · 2017Article
- Reverse Transcription in the Saccharomyces cerevisiae Long-Terminal Repeat Retrotransposon Ty3.Viruses · 2017Review
- Convergence of retrotransposons in oomycetes and plants.Mobile DNA · 2017Article
- Detection of treatment-resistant infectious HIV after genome-directed antiviral endonuclease therapy.Antiviral research · 2016Article
- Transcriptionally active LTR retrotransposons in Eucalyptus genus are differentially expressed and insertionally polymorphic.BMC plant biology · 2015Article
- Convergent evolution of ribonuclease h in LTR retrotransposons and retroviruses.Molecular biology and evolution · 2015Article
- Reverse Transcription of Retroviruses and LTR Retrotransposons.Microbiology spectrum · 2015Review
- Retroviral DNA Transposition: Themes and Variations.Microbiology spectrum · 2014Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Retrotransposons are a class of mobile genetic elements that replicate by converting their single-stranded RNA intermediate to double-stranded DNA through the combined DNA polymerase and ribonuclease H (RNase H) activities of the element-encoded reverse transcriptase (RT). Although a wealth of structural information is available for lentiviral and gammaretroviral RTs, equivalent studies on counterpart enzymes of long terminal repeat (LTR)-containing retrotransposons, from which they are evolutionarily derived, is lacking. In this study, we report the first crystal structure of a complex of RT from the Saccharomyces cerevisiae LTR retrotransposon Ty3 in the presence of its polypurine tract-containing RNA-DNA hybrid. In contrast to its retroviral counterparts, Ty3 RT adopts an asymmetric homodimeric architecture whose assembly is substrate dependent. Moreover, our structure and biochemical data suggest that the RNase H and DNA polymerase activities are contributed by individual subunits of the homodimer.
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