ArticleMobile DNA2016
The endonuclease domain of the LINE-1 ORF2 protein can tolerate multiple mutations.
Article in Mobile DNA, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- The Translatome of Senescent Cells Revealed by Sequencing Actively Translated mRNA.bioRxiv : the preprint server for biology · 2026Article
- Functional analyses identify the L1 ORF2p Cryptic domain as a hub for intramolecular interfaces required for retrotransposition.Nucleic acids research · 2026Article
- Platy-1 SINEs from Thirteen Diverse Genomes Reveal Callithrichidae Unique Amplification, RecentGenes · 2026Article
- Probing genomic language models: Nucleotide Generative Pretrained Transformer and the role of pretraining in learned representations.Briefings in bioinformatics · 2026Article
- Bioenergetic Model of Retrotransposon Activity in Cancer Cells.Life (Basel, Switzerland) · 2025Article
- Domain Mobility in the ORF2p Complex Revealed by Molecular Dynamics Simulations and Big Data Analysis.International journal of molecular sciences · 2024Article
- Identification and characterization of small molecule inhibitors of the LINE-1 retrotransposon endonuclease.Nature communications · 2024Article
- Article
- Bioinformatic Annotation of Transposon DNA Processing Genes on the Long-Read Genome Assembly ofBioinformatics and biology insights · 2024Article
- A novel role of TRIM28 B box domain in L1 retrotransposition and ORF2p-mediated cDNA synthesis.Nucleic acids research · 2023Article
- New oncogenic functions of LINE1 retroelement as a ceRNA for tumor suppressive microRNA miR-126 on ENPP5.PloS one · 2023Article
- SCIFER: approach for analysis of LINE-1 mRNA expression in single cells at a single locus resolution.Mobile DNA · 2022Article
- Signatures of Selection on Mitonuclear Integrated Genes Uncover Hidden Mitogenomic Variation in Fur Seals.Genome biology and evolution · 2022Article
- Cell fitness screens reveal a conflict between LINE-1 retrotransposition and DNA replication.Nature structural & molecular biology · 2020Article
- Truncated ORF1 proteins can suppress LINE-1 retrotransposition in trans.Nucleic acids research · 2017Article
- Involvement of Conserved Amino Acids in the C-Terminal Region of LINE-1 ORF2p in Retrotransposition.Genetics · 2017Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
backgroundApproximately 17 % of the human genome is comprised of the Long INterspersed Element-1 (LINE-1 or L1) retrotransposon, the only currently active autonomous family of retroelements. Though L1 elements have helped to shape mammalian genome evolution over millions of years, L1 activity can also be mutagenic and result in human disease. L1 expression has the potential to contribute to genomic instability via retrotransposition and DNA double-strand breaks (DSBs). Additionally, L1 is responsible for structural genomic variations induced by other transposable elements such as Alu and SVA, which rely on the L1 ORF2 protein for their propagation. Most of the genomic damage associated with L1 activity originates with the endonuclease domain of the ORF2 protein, which nicks the DNA in preparation for target-primed reverse transcription.
resultsBioinformatic analysis of full-length L1 loci residing in the human genome identified numerous mutations in the amino acid sequence of the ORF2 endonuclease domain. Some of these mutations were found in residues which were predicted to be phosphorylation sites for cellular kinases. We mutated several of these putative phosphorylation sites in the ORF2 endonuclease domain and investigated the effect of these mutations on the function of the full-length ORF2 protein and the endonuclease domain (ENp) alone. Most of the single and multiple point mutations that were tested did not significantly impact expression of the full-length ORF2p, or alter its ability to drive Alu retrotransposition. Similarly, most of those same mutations did not significantly alter expression of ENp, or impair its ability to induce DNA damage and cause toxicity.
conclusionsOverall, our data demonstrate that the full-length ORF2p or the ENp alone can tolerate several specific single and multiple point mutations in the endonuclease domain without significant impairment of their ability to support Alu mobilization or induce DNA damage, respectively.
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