http://purl.uniprot.org/citations/29040705 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/29040705 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/29040705 | http://www.w3.org/2000/01/rdf-schema#comment | "Mitochondrial polycistronic transcripts are extensively processed to give rise to functional mRNAs, rRNAs and tRNAs; starting with the release of tRNA elements through 5'-processing by RNase P (MRPP1/2/3-complex) and 3'-processing by RNase Z (ELAC2). Here, we show using in vitro experiments that MRPP1/2 is not only a component of the mitochondrial RNase P but that it retains the tRNA product from the 5'-processing step and significantly enhances the efficiency of ELAC2-catalyzed 3'-processing for 17 of the 22 tRNAs encoded in the human mitochondrial genome. Furthermore, MRPP1/2 retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA-adding enzyme. Thus, in addition to being an essential component of the RNase P reaction, MRPP1/2 serves as a processing platform for several down-stream tRNA maturation steps in human mitochondria. These findings are of fundamental importance for our molecular understanding of disease-related mutations in MRPP1/2, ELAC2 and mitochondrial tRNA genes."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.org/dc/terms/identifier | "doi:10.1093/nar/gkx902"xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.org/dc/terms/identifier | "doi:10.1093/nar/gkx902"xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/author | "Sridhara S."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/author | "Sridhara S."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/author | "Reinhard L."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/author | "Reinhard L."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/author | "Haellberg B.M."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/author | "Haellberg B.M."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/name | "Nucleic Acids Res."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/name | "Nucleic Acids Res."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/pages | "12469-12480"xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/pages | "12469-12480"xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/title | "The MRPP1/MRPP2 complex is a tRNA-maturation platform in human mitochondria."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/title | "The MRPP1/MRPP2 complex is a tRNA-maturation platform in human mitochondria."xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/volume | "45"xsd:string |
http://purl.uniprot.org/citations/29040705 | http://purl.uniprot.org/core/volume | "45"xsd:string |
http://purl.uniprot.org/citations/29040705 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/29040705 |
http://purl.uniprot.org/citations/29040705 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/29040705 |
http://purl.uniprot.org/citations/29040705 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/29040705 |
http://purl.uniprot.org/citations/29040705 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/29040705 |