Novel Mutation and Structural RNA Analysis of the Noncoding RNase <b><i>MRP</i></b> Gene in Cartilage-Hair Hypoplasia [PDF]
Mol Syndromol, 2015 Imane Cherkaoui Jaouad +5 more
semanticscholar +3 more sources
Role of RNase MRP in Viral RNA Degradation and RNA Recombination [PDF]
J Virol, 2010 ABSTRACT RNA degradation, together with RNA synthesis, controls the steady-state level of viral RNAs in infected cells. The endoribonucleolytic cleavage of viral RNA is important not only for viral RNA degradation but for RNA recombination as well, due to the participation of some RNA degradation products in the RNA recombination
H. M. Jaag +3 more
semanticscholar +5 more sources
Composition and RNA binding specificity of metazoan RNase MRP
bioRxivRibonuclease (RNase) MRP is a conserved RNA-based enzyme that is essential for maturation of ribosomal RNA (rRNA) in eukaryotes. However, the composition and RNA substrate specificity of this multisubunit ribonucleoprotein complex in higher eukaryotes ...
Yuan Liu +8 more
semanticscholar +4 more sources
Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components [PDF]
RNA, 2010 RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm. Cytoplasmic RNase MRP is the nucleolar enzyme that is transiently relocalized
Qiaosheng Lu +3 more
semanticscholar +3 more sources
A Novel Model for the RNase MRP-Induced Switch between the Formation of Different Forms of 5.8S rRNA [PDF]
Int J Mol Sci, 2021 Processing of the RNA polymerase I pre-rRNA transcript into the mature 18S, 5.8S, and 25S rRNAs requires removing the “spacer” sequences. The canonical pathway for the removal of the ITS1 spacer involves cleavages at the 3′ end of 18S rRNA and at two ...
Xiao Li, J. Zengel, L. Lindahl
semanticscholar +2 more sources
Coevolution of RNA and protein subunits in RNase P and RNase MRP, two RNA processing enzymes [PDF]
J Biol ChemBin Zhou +5 more
semanticscholar +3 more sources
Targeted CRISPR disruption reveals a role for RNase MRP RNA in human preribosomal RNA processing [PDF]
Genes Dev, 2017 In this study, Goldfarb et al. used CRISPR–Cas9 genome editing to eliminate MRP RNA—a ribonucleoprotein complex with an RNA subunit that is conserved across eukarya—in the majority of cells.
Katherine C. Goldfarb, T. Cech
semanticscholar +2 more sources
A nuclear function for RNase MRP. [PDF]
Proceedings of the National Academy of Sciences, 1994 The site-specific endoribonuclease RNase MRP was first identified 7 years ago as an RNA-processing activity in mammalian cells (1, 2). In the original description of this ribonucleoprotein, as isolated from either mouse or human cells, it was shown that the enzyme had the capacity to cleave RNA in a sequence-specific manner that matched one of the ...
David A. Clayton
openalex +4 more sources
Of proteins and RNA: The RNase P/MRP family [PDF]
RNA, 2010 Nuclear ribonuclease (RNase) P is a ubiquitous essential ribonucleoprotein complex, one of only two known RNA-based enzymes found in all three domains of life. The RNA component is the catalytic moiety of RNases P across all phylogenetic domains; it contains a well-conserved core, whereas peripheral structural elements are diverse.
Olga Esakova, Andrey S. Krasilnikov
openalex +4 more sources
The rRNA methyltransferase Bud23 shows functional interaction with components of the SSU processome and RNase MRP. [PDF]
RNA, 2013 Bud23 is responsible for the conserved methylation of G1575 of 18S rRNA, in the P-site of the small subunit of the ribosome. bud23Δ mutants have severely reduced small subunit levels and show a general failure in cleavage at site A2 during rRNA ...
Richa Sardana +2 more
semanticscholar +2 more sources