Heterodimerization of the human RNase P/MRP subunits Rpp20 and Rpp25 is a prerequisite for interaction with the P3 arm of RNase MRP RNA [PDF]
Nucleic Acids Res, 2010 Rpp20 and Rpp25 are two key subunits of the human endoribonucleases RNase P and MRP. Formation of an Rpp20–Rpp25 complex is critical for enzyme function and sub-cellular localization.
Alex F. Drake +66 more
core +12 more sources
RNase MRP cleaves pre-tRNASer-Met in the tRNA maturation pathway. [PDF]
PLoS ONE, 2014 Ribonuclease mitochondrial RNA processing (RNase MRP) is a multifunctional ribonucleoprotein (RNP) complex that is involved in the maturation of various types of RNA including ribosomal RNA.
Yuichiro Saito +8 more
doaj +3 more sources
Wnt activated β-catenin and YAP proteins enhance the expression of non-coding RNA component of RNase MRP in colon cancer cells [PDF]
Oncotarget, 2015 RMRP, the RNA component of mitochondrial RNA processing endoribonuclease, is a non-coding RNA (ncRNA) part of the RNase MRP complex functioning in mitochondrial and ribosomal RNA processing.
Jinjoo Park, Sunjoo Jeong
semanticscholar +4 more sources
Interactions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture [PDF]
Nucleic Acids Research, 2007 Ribonuclease MRP is an endonuclease, related to RNase P, which functions in eukaryotic pre-rRNA processing. In Saccharomyces cerevisiae, RNase MRP comprises an RNA subunit and ten proteins.
Aspinall, Tanya V. +7 more
core +7 more sources
Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP [PDF]
Cell, 2016 Telomerase is the ribonucleoprotein enzyme that replenishes telomeric DNA and maintains genome integrity. Minimally, telomerase activity requires a templating RNA and a catalytic protein. Additional proteins are required for activity on telomeres in vivo. Here, we report that the Pop1, Pop6, and Pop7 proteins, known components of RNase P and RNase MRP,
B. Lemieux +6 more
semanticscholar +6 more sources
Conserved and variable domains of RNase MRP RNA [PDF]
RNA Biology, 2009 Ribonuclease MRP is a eukaryotic ribonucleoprotein complex consisting of one RNA molecule and 7-10 protein subunits. One important function of MRP is to catalyze an endonucleolytic cleavage during processing of rRNA precursors. RNase MRP is evolutionary related to RNase P which is critical for tRNA processing.
Marcela Dávila López +2 more
semanticscholar +5 more sources
Molecular determinants of RNase MRP specificity and function
bioRxivRNase MRP and RNase P are evolutionarily related complexes that facilitate rRNA and tRNA biogenesis, respectively. The two enzymes share nearly all protein subunits and have evolutionarily related catalytic RNAs.
Eric M. Smith +3 more
semanticscholar +4 more sources
Small RNAs derived from lncRNA RNase MRP have gene-silencing activity relevant to human cartilage–hair hypoplasia [PDF]
Hum Mol Genet, 2014 Post-transcriptional processing of some long non-coding RNAs (lncRNAs) reveals that they are a source of miRNAs. We show that the 268-nt non-coding RNA component of mitochondrial RNA processing endoribonuclease, (RNase MRP), is the source of at least two
Leslie E. Rogler +12 more
semanticscholar +4 more sources
RNase MRP RNA and RNase P activity in plants are associated with a Pop1p containing complex [PDF]
Nucleic Acids Res, 2012 RNase P processes the 5′-end of tRNAs. An essential catalytic RNA has been demonstrated in Bacteria, Archaea and the nuclei of most eukaryotes; an organism-specific number of proteins complement the holoenzyme.
Mario Krehan +4 more
semanticscholar +7 more sources
Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP [PDF]
RNA, 2011 Ribonuclease (RNase) MRP is a multicomponent ribonucleoprotein complex closely related to RNase P. RNase MRP and eukaryotic RNase P share most of their protein components, as well as multiple features of their catalytic RNA moieties, but have distinct ...
Anna Perederina +5 more
semanticscholar +3 more sources