ArticleProceedings of the National Academy of Sciences of the United States of America2009
Non-LTR retrotransposons encode noncanonical RRM domains in their first open reading frame.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
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Who cites it
103 citing papers in PubMed, 162 citations in OpenAlex.
- Ancient Persistence and Newfound Diversity of CR1-Group Retrotransposons Across Vertebrates.Genome biology and evolution · 2026Article
- Functional analyses identify the L1 ORF2p Cryptic domain as a hub for intramolecular interfaces required for retrotransposition.Nucleic acids research · 2026Article
- A phylogenetic estimate of canine retrotransposition rates based on genome assembly comparisons.Mobile DNA · 2026Article
- An Alternative DNA Endonuclease Activity is Associated with the LINE-1 ORF2-encoded Protein.bioRxiv : the preprint server for biology · 2026Article
- Characterizing Complex Nucleic Acid Interactions of LINE1 ORF1p by Single-Molecule Force Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Review
- A phylogenetic estimate of canine retrotransposition rates based on genome assembly comparisons.bioRxiv : the preprint server for biology · 2025Article
- Birth of protein-coding exons by ancient domestication of LINE-1 retrotransposon.Genome research · 2025Article
- LINE-1 ribonucleoprotein condensates bind DNA to enable nuclear entry during mitosis.Science advances · 2025Article
- Maximal inhibitory effect of MOV10 on LINE-1 retrotransposition requires both the MOV10/LINE-1 association and granule formation.PLoS genetics · 2025Article
- Diverse single-stranded nucleic acid binding proteins enable both stable protection and rapid exchange required for biological function.QRB discovery · 2025Article
- Retrotransposition-competent L1s are increased in the genomes of individuals with amyotrophic lateral sclerosis.Experimental biology and medicine (Maywood, N.J.) · 2025Article
- L1-ORF1p nucleoprotein can rapidly assume distinct conformations and simultaneously bind more than one nucleic acid.Nucleic acids research · 2024Article
- Article
- LINE-1 retrotransposition and its deregulation in cancers: implications for therapeutic opportunities.Genes & development · 2023Review
- Co-expression of distinct L1 retrotransposon coiled coils can lead to their entanglement.Mobile DNA · 2023Article
- Locus-resolution analysis of L1 regulation and retrotransposition potential in mouse embryonic development.Genome research · 2023Article
- Functional annotation of a hugely expanded nanos repertoire in Lytechinus variegatus, the green sea urchin.Molecular reproduction and development · 2023Article
- Article
- The L1-ORF1p coiled coil enables formation of a tightly compacted nucleic acid-bound complex that is associated with retrotransposition.Nucleic acids research · 2022Article
43 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Non-LTR retrotransposons (NLRs) are a unique class of mobile genetic elements that have significant impact on the evolution of eukaryotic genomes. However, the molecular details and functions of their encoded proteins, in particular of the accessory ORF1p proteins, are poorly understood. Here, we identify noncanonical RNA-recognition-motifs (RRMs) in several phylogenetically unrelated NLR ORF1p proteins. This provides an explanation for their RNA-binding properties and clearly shows that they are not related to the retroviral nucleocapsid protein Gag, despite the frequent presence of CCHC zinc knuckles. In particular, we characterize the ORF1p protein of the human long interspersed nuclear element 1 (LINE-1 or L1). We show that L1ORF1p is a multidomain protein, consisting of a coiled coil (cc), RRM, and C-terminal domain (CTD). Most importantly, we solved the crystal structure of the RRM domain, which is characterized by extended loops stabilized by unique salt bridges. Furthermore, we demonstrate that L1ORF1p trimerizes via its N-terminal cc domain, and we suggest that this property is functionally important for all homologues. The formation of distinct complexes with single-stranded nucleic acids requires the presence of the RRM and CTD domains on the same polypeptide chain as well as their close cooperation. Finally, the phylogenetic analysis of mammalian L1ORF1p shows an ancient origin of the RRM domain and supports a modular evolution of NLRs.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.