ArticleJournal of molecular biology2007
Three-dimensional structure determined for a subunit of human tRNA splicing endonuclease (Sen15) reveals a novel dimeric fold.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- A role of protein conformational dynamics in mammalian DNA methylation.Structural dynamics (Melville, N.Y.) · 2026Review
- Functional Insight into hTRIR.Current molecular medicine · 2024Article
- Structural basis of substrate recognition by human tRNA splicing endonuclease TSEN.Nature structural & molecular biology · 2023Article
- Structural basis for pre-tRNA recognition and processing by the human tRNA splicing endonuclease complex.Nature structural & molecular biology · 2023Article
- Mediation of the Same Epigenetic and Transcriptional Effect by Independent Osteoarthritis Risk-Conferring Alleles on a Shared Target Gene, COLGALT2.Arthritis & rheumatology (Hoboken, N.J.) · 2023Article
- Recent insights into the structure, function, and regulation of the eukaryotic transfer RNA splicing endonuclease complex.Wiley interdisciplinary reviews. RNA · 2022Review
- Assembly defects of human tRNA splicing endonuclease contribute to impaired pre-tRNA processing in pontocerebellar hypoplasia.Nature communications · 2021Article
- Reconstitution of the human tRNA splicing endonuclease complex: insight into the regulation of pre-tRNA cleavage.Nucleic acids research · 2020Article
- Recent Insights Into the Structure, Function, and Evolution of the RNA-Splicing Endonucleases.Frontiers in genetics · 2019Review
- Autosomal-Recessive Mutations in the tRNA Splicing Endonuclease Subunit TSEN15 Cause Pontocerebellar Hypoplasia and Progressive Microcephaly.American journal of human genetics · 2016Article
- tRNA gene diversity in the three domains of life.Frontiers in genetics · 2014Review
- Sequence, structure and functional diversity of PD-(D/E)XK phosphodiesterase superfamily.Nucleic acids research · 2012Article
- Structural basis for RNA recognition by a type II poly(A)-binding protein.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- The dawn of dominance by the mature domain in tRNA splicing.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Splicing of eukaryal intron-containing tRNAs requires the action of the heterotetrameric splicing endonuclease, which is composed of two catalytic subunits, Sen34 and Sen2, and two structural subunits, Sen15 and Sen54. Here we report the solution structure of the human tRNA splicing endonuclease subunit HsSen15. To facilitate the structure determination, we removed the disordered 35 N-terminal and 14 C-terminal residues of the full-length protein to produce HsSen15(36-157). The structure of HsSen15(36-157), the first for a subunit of a eukaryal splicing endonuclease, revealed that the protein possesses a novel homodimeric fold. Each monomer consists of three alpha-helices and a mixed antiparallel/parallel beta-sheet, arranged in a topology similar to that of the C-terminal domain of Methanocaldococcus jannaschii endonuclease. The dimeric interface is dominated by a beta-barrel structure, formed by face-to-face packing of two, three-stranded beta-sheets. Each of the beta-sheets results from reciprocal parallel pairing of one beta-strand from one subunit with two other beta-strands from the symmetric subunit. The structural model provides insights into the functional assembly of the human tRNA splicing endonuclease.
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