Journal
NATURE
Volume 511, Issue 7507, Pages 104-U508Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature13284
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Funding
- Fonds zur Forderung der wissenschaftlichen Forschung [P24687]
- GEN-AU 3 research programme [820982]
- Institute of Molecular Biotechnology of the Austrian Academy of Sciences
- Austrian Science Fund (FWF) [P 24687] Funding Source: researchfish
- Austrian Science Fund (FWF) [W1207, P24687] Funding Source: Austrian Science Fund (FWF)
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RNA ligases have essential roles in many cellular processes in eukaryotes, archaea and bacteria, including in RNA repair(1,2) and stress-induced splicing of messenger RNA(3). In archaea and eukaryotes, RNA ligases also have a role in transfer RNA splicing to generate functional tRNAs required for protein synthesis(4-7). 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(8). 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.
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