Results 151 to 160 of about 108,983 (200)
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2001
Publisher Summary Ribonuclease P is a ribonucleoprotein nuclease required for the site-specific cleavage of the 5′ leader sequence of precursor tRNAs. In eubacteria, the RNA subunit of RNase P is the catalytic moiety and is capable of processing precursor tRNA in the presence of divalent metal ions.
N, Jarrous, S, Altman
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Publisher Summary Ribonuclease P is a ribonucleoprotein nuclease required for the site-specific cleavage of the 5′ leader sequence of precursor tRNAs. In eubacteria, the RNA subunit of RNase P is the catalytic moiety and is capable of processing precursor tRNA in the presence of divalent metal ions.
N, Jarrous, S, Altman
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The varieties of ribonuclease P
Trends in Biochemical Sciences, 1992Ribonuclease P is a ribozyme involved in tRNA processing that is present in all cells and organelles that synthesize tRNA. Most of our understanding of ribonuclease P derives from studies of the bacterial enzyme. This enzyme has been characterized biochemically and a secondary structure for the RNA subunit has been proposed.
S C, Darr, J W, Brown, N R, Pace
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Ribonuclease P: a ribonucleoprotein enzyme
Current Opinion in Chemical Biology, 2000The ribonucleoprotein ribonuclease P catalyzes the hydrolysis of a specific phosphodiester bond in precursor tRNA to form the mature 5' end of tRNA. Recent studies have shed light on the structures of RNase-P-RNA-P-protein and RNase-P-RNA-precursor-tRNA complexes, as well as on the positions of catalytic metal ions, emphasizing the importance of the ...
J C, Kurz, C A, Fierke
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The enigma of ribonuclease P evolution
Trends in Genetics, 2003The 5'-end maturation of tRNAs is catalyzed by the ribonucleoprotein enzyme ribonuclease P (RNase P) in all organisms. Here we provide, for the first time, a comprehensive overview on the representation of individual RNase P protein homologs within the Eukarya and Archaea.
Enno, Hartmann, Roland K, Hartmann
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Ribonuclease P structure and function inArchaea
Molecular Biology Reports, 1996An important approach to understanding RNA-based catalytic function by ribonuclease P is the investigation of its evolutionary diversity in structure and function. Because RNase P enzymes from all organisms are thought to share common ancestry, the fundamental features of structure and biochemistry should be conserved in all of its modern forms.
J W, Brown, E S, Haas
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Recent studies of ribonuclease P.
The FASEB Journal, 1993RNase P is an essential enzyme that is required for the biosynthesis of tRNA. It is composed of RNA and protein subunits. The RNA subunit of the enzyme derived from eubacterial sources can carry out the catalytic function by itself in vitro. Current studies of RNase P focus on structure-function relationships with respect to interactions of the RNA ...
S, Altman, L, Kirsebom, S, Talbot
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Mitochondrial ribonuclease P activity of Trypanosoma brucei
Molecular and Biochemical Parasitology, 2001Ribonuclease P (RNase P) is an essential enzyme that cleaves the 5' leader sequences of precursor tRNAs (pre-tRNAs) to generate mature tRNAs. The RNase P-like activity from Trypanosoma brucei mitochondria (mtRNase P) was purified over 10000-fold by sequential column chromatography.
R, Salavati, A K, Panigrahi, K D, Stuart
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Structure and evolution of ribonuclease P RNA
Biochimie, 1991Eubacterial RNase P contains a catalytic RNA that cleaves 5' leader sequences from precursor tRNAs. We review the current understanding of RNase P RNA structure and evolution, from the perspective of phylogenetic comparative analysis.
J W, Brown, N R, Pace
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Activation of Bacterial Ribonuclease P by Macrolides
Biochemistry, 2008The effect of macrolide antibiotic spiramycin on RNase P holoenzyme and M1 RNA from Escherichia coli was investigated. Ribonuclease P (RNase P) is a ribozyme that is responsible for the maturation of 5' termini of tRNA molecules. Spiramycin revealed a dose-dependent activation on pre-tRNA cleavage by E. coli RNase P holoenzyme and M1 RNA. The K s and V
Toumpeki, Chrisavgi +4 more
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Escherichia coli Ribonuclease P
2001Publisher Summary Ribonuclease P is an endoribonuclease responsible for the maturation of the 5′ termini of the majority of all known tRNAs in all cell types studied to date. In Escherichia coli, RNase P consists of an RNA subunit, Ml RNA, and a small basic protein, C5.
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