Results 251 to 260 of about 25,923,055 (288)
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Eukaryote RNase P and RNase MRP
2009Ribonuclease 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 +2 more
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A novel protein shared by RNase MRP and RNase P
RNA (New York, N.Y.), 1997We 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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Definition of the Th/ To ribonucleoprotein by RNase P and RNase MRP
Molecular Biology Reports, 1993We 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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Molecular BioSystems, 2007
Abstract Major progress in the study of RNase P has resulted from crystallography of bacterial catalytic subunits and the discovery of catalytic activity in eukaryotes. Several new substrates have also been identified, primarily in bacteria but also in yeast.
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Abstract Major progress in the study of RNase P has resulted from crystallography of bacterial catalytic subunits and the discovery of catalytic activity in eukaryotes. Several new substrates have also been identified, primarily in bacteria but also in yeast.
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Pop3p Is Essential for the Activity of the RNase MRP and RNase P Ribonucleoproteins in Vivo
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.
David Tollervey
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The RNase P ofDictostyelium discoideum
Molecular Biology Reports, 1996Ribonuclease P (RNase P) is a key enzyme involved in tRNA biosynthesis. It catalyses the endonucleolytic cleavage of nearly all tRNA precursors to produce 5'-end matured tRNA. RNase P activity has been found in all organisms examined, from bacteria to mammals.
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RNase P in Research and Therapy
Nature Biotechnology, 1995Fooling the catalytic RNA subunit into recognizing nonnatural substrates may have important implications for ...
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Molecular Biology Reports, 1996
Molecular investigations in mitochondria of higher plants have to take in account the complicated genomic structure of these organelles and their complex mode of gene expression. Recently tRNA processing activities and particularly RNase P-like activities have been described for mitochondria of mono- and dicot plants.
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Molecular investigations in mitochondria of higher plants have to take in account the complicated genomic structure of these organelles and their complex mode of gene expression. Recently tRNA processing activities and particularly RNase P-like activities have been described for mitochondria of mono- and dicot plants.
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Annual Review of Biophysics, 2013
Ribonuclease P (RNase P) is one of the first ribozymes discovered and it is found in all phylogenetic groups. It is responsible for processing the 5′ end of pre-tRNAs as well as other RNA molecules. RNase P is formed by an RNA molecule responsible for catalysis and one or more proteins.
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Ribonuclease P (RNase P) is one of the first ribozymes discovered and it is found in all phylogenetic groups. It is responsible for processing the 5′ end of pre-tRNAs as well as other RNA molecules. RNase P is formed by an RNA molecule responsible for catalysis and one or more proteins.
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RNase P RNA ofMycoplasma capricolum
Molecular Biology Reports, 1996There are at least six small stable RNAs in Mycoplasma capricolum cells besides tRNAs and rRNAs. One of them, MCS5 RNA, is a homolog of RNase P RNA. The predicted secondary structure of this RNA is essentially the same as that of other eubacterial RNase P RNAs. MCS5 RNA is more similar to the RNase P RNA of B. Subtilis than to that of E. coli.
C, Ushida, D, Izawa, A, Muto
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