ArticleNucleic acids research2014
Identification of RNA binding motifs in the R2 retrotransposon-encoded reverse transcriptase.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Functional analyses identify the L1 ORF2p Cryptic domain as a hub for intramolecular interfaces required for retrotransposition.Nucleic acids research · 2026Article
- Rewriting the genome: harnessing R2 retrotransposons for precise DNA insertion.Frontiers in genome editing · 2026Review
- Biology and utilization of R2 retrotransposons.RNA biology · 2025Review
- Structure and biochemistry-guided engineering of an all-RNA system for DNA insertion with R2 retrotransposons.Nature communications · 2025Article
- Distinct and overlapping RNA determinants for binding and target-primed reverse transcription by Bombyx mori R2 retrotransposon protein.Nucleic acids research · 2024Article
- Article
- Structure of the R2 non-LTR retrotransposon initiating target-primed reverse transcription.Science (New York, N.Y.) · 2023Article
- Article
- Impaired function of rDNA transcription initiation machinery leads to derepression of ribosomal genes with insertions of R2 retrotransposon.Nucleic acids research · 2022Article
- The non-LTR retrotransposons of Entamoeba histolytica: genomic organization and biology.Molecular genetics and genomics : MGG · 2022Review
- Template-switching mechanism of a group II intron-encoded reverse transcriptase and its implications for biological function and RNA-Seq.The Journal of biological chemistry · 2019Article
- Current Perspectives of Telomerase Structure and Function in Eukaryotes with Emerging Views on Telomerase in Human Parasites.International journal of molecular sciences · 2018Review
- The group II intron maturase: a reverse transcriptase and splicing factor go hand in hand.Current opinion in structural biology · 2017Review
- Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo.Protoplasma · 2017Article
- Involvement of Conserved Amino Acids in the C-Terminal Region of LINE-1 ORF2p in Retrotransposition.Genetics · 2017Article
- Globular domain structure and function of restriction-like-endonuclease LINEs: similarities to eukaryotic splicing factor Prp8.Mobile DNA · 2017Article
- Evolutionary perspectives of telomerase RNA structure and function.RNA biology · 2016Review
- Identification of L1 ORF2p sequence important to retrotransposition using Bipartile Alu retrotransposition (BAR).Nucleic acids research · 2016Article
- Crystal structures of a group II intron maturase reveal a missing link in spliceosome evolution.Nature structural & molecular biology · 2016Article
- Endonuclease domain of non-LTR retrotransposons: loss-of-function mutants and modeling of the R2Bm endonuclease.Nucleic acids research · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
R2 non-LTR retrotransposons insert at a specific site in the 28S rRNA genes of many animal phyla. R2 elements encode a single polypeptide with reverse transcriptase, endonuclease and nucleic acid binding domains. Integration involves separate cleavage of the two DNA strands at the target site and utilization of the released 3' ends to prime DNA synthesis. Critical to this integration is the ability of the protein to specifically bind 3' and 5' regions of the R2 RNA. In this report, alanine mutations in two conserved motifs N-terminal to the reverse transcriptase domain were generated and shown to result in proteins that retained the ability to cleave the first strand of the DNA target, to reverse transcribe RNA from an annealed primer and to displace annealed RNA when using DNA as a template. However, the mutant proteins had greatly reduced ability to bind 3' and 5' RNA in mobility shift assays, use the DNA target to prime reverse transcription and conduct second-strand DNA cleavage. These motifs thus appear to participate in all activities of the R2 protein known to require specific RNA binding. The similarity of these R2 RNA binding motifs to those of telomerase and group II introns is discussed.
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