RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/24870230http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24870230http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24870230http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.org/dc/terms/identifier"doi:10.1038/nature13284"xsd:string
http://purl.uniprot.org/citations/24870230http://purl.org/dc/terms/identifier"doi:10.1038/nature13284"xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/author"Martinez J."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/author"Martinez J."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/author"Schleiffer A."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/author"Schleiffer A."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/author"Jurkin J."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/author"Jurkin J."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/author"Popow J."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/author"Popow J."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/pages"104-107"xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/pages"104-107"xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/title"Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing factors."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/title"Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing factors."xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/volume"511"xsd:string
http://purl.uniprot.org/citations/24870230http://purl.uniprot.org/core/volume"511"xsd:string
http://purl.uniprot.org/citations/24870230http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24870230
http://purl.uniprot.org/citations/24870230http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24870230