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Nature, 2008
The universality of ribonuclease P (RNase P), the ribonucleoprotein essential for transfer RNA (tRNA) 5' maturation, is challenged in the archaeon Nanoarchaeum equitans. Neither extensive computational analysis of the genome nor biochemical tests in cell extracts revealed the existence of this enzyme.
Lennart, Randau +2 more
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The universality of ribonuclease P (RNase P), the ribonucleoprotein essential for transfer RNA (tRNA) 5' maturation, is challenged in the archaeon Nanoarchaeum equitans. Neither extensive computational analysis of the genome nor biochemical tests in cell extracts revealed the existence of this enzyme.
Lennart, Randau +2 more
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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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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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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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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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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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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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Yeast mitochondrial RNase P: an unusual member of the RNase P enzyme family
1995We 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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Characterization of RNase P RNA Activity
2012The 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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Further characterization of human RNase MRP/RNase P and related autoantibodies
Molecular Biology Reports, 1998We 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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