The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins. [PDF]
Two forms of the yeast 5.8S rRNA are generated from a large precursor by distinct processing pathways. Cleavage at site A3 is required for synthesis of the major, short form, designated 5.8S(S), but not for synthesis of the long form, 5.8S(L).
Zoi Lygerou+4 more
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Architecture and Function of the Human Endonucleases RNase P and RNase MRP [PDF]
AbstractIn the past decade, important advances have been made in our knowledge of the composition of human RNase MRP and RNase P complexes. Both ribonucleoprotein particles function as endonucleases and contain RNA components that are structurally related.
Hans van Eenennaam+3 more
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Stability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP [PDF]
Pop1 and 6 are subunits of RNase P and RNase MRP, which process ribosomal and tRNAs. The authors show that when Pop1 and 6 are impaired, the telomerase subunit Est1 binds telomerase RNA at normal levels, but the binding is unstable.
P. Daniela Garcia+7 more
doaj +2 more sources
Whole-exome re-sequencing in a family quartet identifies POP1 mutations as the cause of a novel skeletal dysplasia. [PDF]
Recent advances in DNA sequencing have enabled mapping of genes for monogenic traits in families with small pedigrees and even in unrelated cases. We report the identification of disease-causing mutations in a rare, severe, skeletal dysplasia, studying a
Evgeny A Glazov+7 more
doaj +8 more sources
hPop5, a Protein Subunit of the Human RNase MRP and RNase P Endoribonucleases [PDF]
The RNase MRP and RNase P particles both function as endoribonucleases. RNase MRP has been implicated in the processing of precursor-rRNA, whereas RNase P has been shown to function in the processing of pre-tRNA. Both ribonucleoprotein particles have an RNA component that can be folded into a similar secondary structure and share several protein ...
Hans van Eenennaam+4 more
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Characterization and Purification of Saccharomyces cerevisiae RNase MRP Reveals a New Unique Protein Component [PDF]
In the yeast Saccharomyces cerevisiae, RNase mitochondrial RNA processing (MRP) is an essential endoribonuclease that consists of one RNA component and at least nine protein components.
Kelly Salinas+3 more
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RNase MRP RNA and human genetic diseases [PDF]
RNase MRP RNA is the RNA subunit of the RNase mitochondrial RNA processing (MRP) enzyme complex that is involved in multiple cellular RNA processing events. Mutations on RNase MRP RNA gene (RMRP) cause a recessively inherited developmental disorder, cartilage-hair hypoplasia (CHH).
Allison N. Martin, Yong Li
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Genetic changes in the RNA components of RNase MRP and RNase P in Schmid metaphyseal chondrodysplasia [PDF]
The Schmid type of metaphyseal chondrodysplasia (MCDS) is generally due to mutations in COL10A1 encoding for type X collagen of cartilage.We performed a study on the genes coding for the RNA components of RNase MRP (MRPR) and RNase P (H1RNA) among 20 patients with diagnosis of MCDS and no mutations in COL10A1.Two patients were found to be homozygous ...
Maaret Ridanpää
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AbstractThe human RNase MRP complex consists of a catalytic RNA and several protein components. RNase MRP is a ubiquitously expressed eukaryotic endoribonuclease that cleaves various RNAs, including ribosomal, messenger, and mitochondrial RNAs, in a highly specific fashion.
S. Mattijssen, T. Welting, G. Pruijn
semanticscholar +5 more sources
Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP [PDF]
Ribonuclease P (RNase P) is a ribonucleoprotein enzyme that cleaves precursor tRNA transcripts to give mature 5' ends. RNase P in eubacteria has a large, catalytic RNA subunit and a small protein subunit that are required for precursor tRNA cleavage in ...
Joel R. Chamberlain+3 more
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