The RNA of RNase MRP is required for normal processing of ribosomal RNA.
S Chu, RH Archer, JM Zengel… - Proceedings of the …, 1994 - National Acad Sciences
We have isolated clones which complement the temperature sensitivity and abnormal rRNA
processing pattern of the rrp2-2 mutant of Saccharomyces cerevisiae we previously …
processing pattern of the rrp2-2 mutant of Saccharomyces cerevisiae we previously …
Probing the structure of Saccharomyces cerevisiae RNase MRP
SC Walker, TV Aspinall, JMB Gordon, JM Avis - 2005 - portlandpress.com
In yeast, RNase MRP (mitochondrial RNA processing), a ribonucleoprotein precursor rRNA
processing enzyme, possesses one putatively catalytic RNA and ten protein subunits and is …
processing enzyme, possesses one putatively catalytic RNA and ten protein subunits and is …
Characterization of a unique protein component of yeast RNase MRP: an RNA-binding protein with a zinc-cluster domain.
ME Schmitt, DA Clayton - Genes & Development, 1994 - genesdev.cshlp.org
RNase MRP is a ribonucleoprotein endoribonuclease that has been shown to cleave
mitochondrial primer RNA sequences from a variety of sources. Most of the RNase MRP …
mitochondrial primer RNA sequences from a variety of sources. Most of the RNase MRP …
A conserved element in the yeast RNase MRP RNA subunit can participate in a long-range base-pairing interaction
SC Walker, JM Avis - Journal of molecular biology, 2004 - Elsevier
RNase MRP is a ribonucleoprotein endoribonuclease involved in eukaryotic pre-rRNA
processing. The enzyme possesses a putatively catalytic RNA subunit, structurally related to …
processing. The enzyme possesses a putatively catalytic RNA subunit, structurally related to …
A nuclear function for RNase MRP.
DA Clayton - Proceedings of the National Academy of …, 1994 - National Acad Sciences
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 …
processing activity in mammalian cells (1, 2). In the original description of this …
[引用][C] A role for RNase MRP in mitochondrial RNA processing
JN Topper, JL Bennett, DA Clayton - Cell, 1992 - Elsevier
The basic mode of mammalian mitochondrial DNA (mtDNA) replication has been
established (Clayton, 1982), and the predominant control region for both replication and …
established (Clayton, 1982), and the predominant control region for both replication and …
Characterization of ribonuclease MRP function
T Cai, ME Schmitt - Methods in enzymology, 2001 - Elsevier
Publisher Summary Ribonuclease (RNase) MRP is a ribonucleoprotein endoribonuclease
that cleaves an RNA sequence in a site-specific manner. The enzyme has two known RNA …
that cleaves an RNA sequence in a site-specific manner. The enzyme has two known RNA …
RNase MRP/RNase P: a structure-function relation conserved in evolution?
R Karwan - FEBS letters, 1993 - Elsevier
Abstract RNase P and RNase MRP are related ribonucleoproteins. RNase MRP processes
mitochondrial precursor-(primer) RNAs, whereas RNase P cleaves precursor-tRNAs to …
mitochondrial precursor-(primer) RNAs, whereas RNase P cleaves precursor-tRNAs to …
RNase MRP is required for entry of 35S precursor rRNA into the canonical processing pathway
L Lindahl, A Bommankanti, X Li, L Hayden, A Jones… - Rna, 2009 - rnajournal.cshlp.org
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 …
during ribosome biogenesis. Previous experiments suggested that RNase MRP makes a …
Nuclear RNase MRP processes RNA at multiple discrete sites: interaction with an upstream G box is required for subsequent downstream cleavages.
R Karwan, JL Bennett, DA Clayton - Genes & development, 1991 - genesdev.cshlp.org
RNase MRP is a site-specific endoribonuclease that processes primer RNA from the leading-
strand origin of mammalian mitochondrial DNA replication. It is present in active form as …
strand origin of mammalian mitochondrial DNA replication. It is present in active form as …