Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing factors
Autor: | Alexander Schleiffer, Javier Martinez, Johannes Popow, Jennifer Jurkin |
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Rok vydání: | 2014 |
Předmět: |
Genetics
Multidisciplinary Cell Survival RNA Splicing Intron Proteins RNA Ligase (ATP) RNA-Binding Proteins RNA Biology Non-coding RNA Article Post-transcriptional modification DEAD-box RNA Helicases Evolution Molecular RNA Transfer Multienzyme Complexes RNA editing Catalytic Domain RNA splicing Humans Signal recognition particle RNA Carrier Proteins Conserved Sequence Small nuclear RNA |
Zdroj: | Nature. 511:104-107 |
ISSN: | 1476-4687 0028-0836 |
Popis: | RNA ligases have essential roles in many cellular processes in eukaryotes, archaea and bacteria, including in RNA repair and stress-induced splicing of messenger RNA. In archaea and eukaryotes, RNA ligases also have a role in transfer RNA splicing to generate functional tRNAs required for protein synthesis. We recently identified the human tRNA splicing ligase, a multimeric protein complex with RTCB (also known as HSPC117, C22orf28, FAAP and D10Wsu52e) as the essential subunit. The functions of the additional complex components ASW (also known as C2orf49), CGI-99 (also known as C14orf166), FAM98B and the DEAD-box helicase DDX1 in the context of RNA ligation have remained unclear. Taking advantage of clusters of eukaryotic orthologous groups, here we find that archease (ARCH; also known as ZBTB8OS), a protein of unknown function, is required for full activity of the human tRNA ligase complex and, in cooperation with DDX1, facilitates the formation of an RTCB-guanylate intermediate central to mammalian RNA ligation. Our findings define a role for DDX1 in the context of the human tRNA ligase complex and suggest that the widespread co-occurrence of archease and RtcB proteins implies evolutionary conservation of their functional interplay. |
Databáze: | OpenAIRE |
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