Results 261 to 270 of about 455,663 (298)
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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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RNase P RNA-mediated catalysis

Biochemical Society Transactions, 2002
The endoribonuclease RNase P is involved in the processing of tRNA precursors to generate mature 5′ termini. The catalytic activity of RNase P is associated with an RNA, RNase P RNA. A specific interaction between the 3′ end of the substrate and RNase P RNA, to form an RNase P RNA-substrate complex, is referred to as the ‘73–294-interaction’.
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Structural Studies of RNase P

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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A view of RNase P

Molecular BioSystems, 2007
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. Our current world should be called the "RNA-protein world" rather than the "protein world".
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The RNase P ofDictostyelium discoideum

Molecular Biology Reports, 1996
Ribonuclease 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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Characterization of RNase P RNA Activity

2012
The principle task of the ubiquitous enzyme RNase P is the generation of mature tRNA 5'-ends by removing precursor sequences from tRNA primary transcripts (Trends Genet 19:561-569, 2003; Crit Rev Biochem Mol Biol 41:77-102, 2006; Trends Biochem Sci 31:333-341, 2006).
Markus, Gössringer   +2 more
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RNase P in Research and Therapy

Nature Biotechnology, 1995
Fooling the catalytic RNA subunit into recognizing nonnatural substrates may have important implications for ...
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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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Yeast mitochondrial RNase P: an unusual member of the RNase P enzyme family

1995
We review here our studies of the tRNA processing enzyme, RNase P. Yeast mitochondrial RNase P contains an AU-rich mitochondrial coded RNA which varies in size in different yeasts. All of these RNAs contain two short sequences with similarity to two sequences found in all RNase P RNAs.
G.-J. Gao   +3 more
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RNase P from Organelles

2009
RNase P is an almost universal enzyme present in Bacteria, Archaea and Eukaryotic nuclei, as well as in mitochondria and chloroplasts. The organellar enzyme shows a great variability in structure and composition. A gene encoding an RNA, homologous to bacterial catalytic RNase P RNA, is found in mitochondria of a diversity of organisms that include ...
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