Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactions. [PDF]
RNA, 2012 Eukaryotic ribonuclease (RNase) P and RNase MRP are closely related ribonucleoprotein complexes involved in the metabolism of various RNA molecules including tRNA, rRNA, and some mRNAs.
E. Khanova +4 more
semanticscholar +2 more sources
Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex [PDF]
Nucleic Acids Research, 2004 The eukaryotic ribonuclease for mitochondrial RNA processing (RNase MRP) is mainly located in the nucleoli and belongs to the small nucleolar ribonucleoprotein (snoRNP) particles.
Tim J. M. Welting
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Phylogenetic analysis of the structure of RNase MRP RNA in yeasts [PDF]
RNA, 2002 RNase MRP is a ribonucleoprotein enzyme involved in processing precursor rRNA in eukaryotes. To facilitate our structure-function analysis of RNase MRP from Saccharomyces cerevisiae, we have determined the likely secondary structure of the RNA component by a phylogenetic approach in which we sequenced all or part of the RNase MRP RNAs from 17 ...
Xing Li +4 more
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hPop4: a new protein subunit of the human RNase MRP and RNase P ribonucleoprotein complexes [PDF]
Nucleic Acids Research, 1999 RNase MRP is a ribonucleoprotein particle involved in the processing of pre-rRNA. The RNase MRP particle is structurally highly related to the RNase P particle, which is involved in pre-tRNA processing. Their RNA components fold into a similar secondary structure and they share several protein subunits.
Hans van Eenennaam
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PLoS ONE, 2012 RNA biogenesis, including biosynthesis and maturation of rRNA, tRNA and mRNA, is a fundamental process that is critical for cell growth, division and differentiation.
Si-Qi Wang +4 more
doaj +3 more sources
Pop3p is essential for the activity of the RNase MRP and RNase P ribonucleoproteins in vivo
The EMBO Journal, 1997 RNase MRP is a ribonucleoprotein (RNP) particle which is involved in the processing of pre-rRNA at site A3 in internal transcribed spacer 1. Although RNase MRP has been analysed functionally, the structure and composition of the particle are not well characterized.
B. Dichtl, D. Tollervey
semanticscholar +5 more sources
Functional equivalence of hairpins in the RNA subunits of RNase MRP and RNase P in Saccharomyces cerevisiae [PDF]
RNA, 2000 RNase MRP and RNase P are both ribonucleoprotein enzymes performing endonucleolytic cleavage of RNA. RNase MRP cleaves at a specific site in the precursor-rRNA transcript to initiate processing of the 5.8S rRNA. RNase P cleaves precursor tRNAs to create the 5' end of the mature tRNAs.
Lasse Lindahl +3 more
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hPop1: an autoantigenic protein subunit shared by the human RNase P and RNase MRP ribonucleoproteins. [PDF]
The EMBO Journal, 1996 The eukaryotic endonucleases RNase P and RNase MRP require both RNA and protein subunits for function. Even though the human RNase P and MRP RNAs were previously characterized, the protein composition of the particles remains unknown. We have identified a human a Caenorhabditis elegans sequence showing homology to yPop1, a protein subunit of the yeast ...
Zoi Lygerou +3 more
semanticscholar +5 more sources
RNase MRP is required for entry of 35S precursor rRNA into the canonical processing pathway. [PDF]
RNA, 2009 RNase MRP is a nucleolar RNA-protein enzyme that participates in the processing of rRNA during ribosome biogenesis. Previous experiments suggested that RNase MRP makes a nonessential cleavage in the first internal transcribed spacer.
L. Lindahl +7 more
semanticscholar +2 more sources
Heterodimerization regulates RNase MRP/RNase P association, localization, and expression of Rpp20 and Rpp25 [PDF]
RNA, 2006 Rpp20 and Rpp25 are subunits of the human RNase MRP and RNase P endoribonucleases belonging to the Alba superfamily of nucleic acid binding proteins. These proteins, which bind very strongly to each other, transiently associate with RNase MRP. Here, we show that the Rpp20-Rpp25 heterodimer is resistant to both high concentrations of salt and a nonionic
Tim J. M. Welting +7 more
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