Results 131 to 140 of about 3,043 (149)

RNase MRP and rRNA processing

Molecular Biology Reports, 1996
RNase MRP is a ribonucleoprotein enzyme with a structure similar to RNase P. It is required for normal processing of precursor rRNA, cleaving it in the Internal Transcribed Spacer 1.
L, Lindahl, J M, Zengel
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Schizosaccharomyces pombe RNase MRP RNA is homologous to metazoan RNase MRP RNAs and may provide clues to interrelationships between RNase MRP and RNase P

Yeast, 1995
AbstractRNase MRP and RNase P ribonucleoproteins are structurally and functionally similar across a large evolutionary distance. To better characterize possible complex interrelationships between these two enzymes, we have employed the fission yeast Schizosaccharomyces pombe. Unlike Saccharomyces cerevisiae, S.
J L, Paluh, D A, Clayton
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A novel protein shared by RNase MRP and RNase P

RNA (New York, N.Y.), 1997
We have isolated suppressors of the temperature-sensitive rRNA processing mutation rrp2-2 in Saccharomyces cerevisiae. A class of extragenic suppressors was mapped to the YBR257w reading frame in the right arm of Chromosome II. Characterization of this gene, renamed POP4, shows that the gene product is necessary both for normal 5.8S rRNA processing and
S, Chu, J M, Zengel, L, Lindahl
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Eukaryote RNase P and RNase MRP

2009
Ribonuclease P (RNase P) is an essential endonuclease that catalyzes the cleavage of the 5′ leader sequence from precursor tRNAs (pre-tRNAs). Most forms of RNase P are ribonucleoproteins and the bacterial enzyme possesses a single catalytic RNA and one small protein.
Scott C. Walker, Michael C. Marvin, David R. Engelke   +2 more
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Probing the structure of Saccharomyces cerevisiae RNase MRP

Biochemical Society Transactions, 2005
In yeast, RNase MRP (mitochondrial RNA processing), a ribonucleoprotein precursor rRNA processing enzyme, possesses one putatively catalytic RNA and ten protein subunits and is highly related to RNase P. Structural analysis of the MRP RNA provides data that closely match a previous secondary-structure model derived from phylogenetic analysis, with the ...
Walker, S. C., Aspinall, T. V., Gordon, J. M B, Avis, J. M.   +3 more
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Definition of the Th/ To ribonucleoprotein by RNase P and RNase MRP

Molecular Biology Reports, 1993
We show that the Th/To ribonucleoprotein is defined by (i) the co-immunoprecipitation of two RNAs, (ii) the co-immunoprecipitation of four major polypeptides and (iii) the quantitative immune recognition of both RNase P and RNase MRP. No serum was found that recognizes either one of these two enzymes exclusively.
W, Rossmanith, R, Karwan
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Further characterization of human RNase MRP/RNase P and related autoantibodies

Molecular Biology Reports, 1998
We characterized a panel of human RNase MRP/RNase P autoantibodies by immunoprecipitation, immunodepletion, immunoaffinity purification and immunoblotting. We report on the protein spectrum that is recognized by RNase MRP/RNase P autoantibodies. We also describe another, related patient serum that based on these assays does not immunoprecipitate RNase ...
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Structural and functional similarities between MRP and RNase P

Molecular Biology Reports, 1996
RNase P, the enzyme response for 5'-end processing of tRNAs and 4.5S RNA, has been extensively characterized from E. coli. The RNA component of E. coli RNase P, without the protein, has the enzymatic activity and is the first true RNA enzyme to be characterized. RNase P and MRP are two distinct nuclear ribonucleoprotein (RNP) particles characterized in
R, Reddy, S, Shimba
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Genetic and biochemical analyses of yeast RNase MRP

Molecular Biology Reports, 1996
RNase MRP cleaves the yeast pre-rRNA at a site in internal transcribed spacer 1 (ITS1) and this cleavage can be reproduced in vitro by the highly purified enzyme. Two protein components (Pop1p and Pop2p) have been identified which are common to yeast RNase MRP and RNase P.
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The yeast,Saccharomyces cerevisiae, RNase P/MRP ribonucleoprotein endoribonuclease family

Molecular Biology Reports, 1996
Ribonuclease P (RNase P) is a ribonucleoprotein responsible for the endonucleolytic cleavage of the 5'-termini of tRNAs. Ribonuclease MRP (RNase MRP) is a ribonucleoprotein that has the ability to cleave both mitochondrial RNA primers presumed to be involved in mitochondrial DNA replication and rRNA precursors for the production of mature rRNAs ...
T H, Reilly, M E, Schmitt
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