Results 291 to 300 of about 112,073 (318)

Ribonuclease P: a ribonucleoprotein enzyme

Current Opinion in Chemical Biology, 2000
The 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, 2003
The 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, 1996
An 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, 1993
RNase 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, 2001
Ribonuclease 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, 1991
Eubacterial 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, 2008
The 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, Vourekas, Anastassios, Kalavrizioti, Dimitra, Stamatopoulou, Vasiliki, Drainas, Denis   +4 more
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Escherichia coli Ribonuclease P

2001
Publisher 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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Long-Range Structure in Ribonuclease P RNA

Science, 1991
Phylogenetic-comparative and mutational analyses were used to elucidate the structure of the catalytically active RNA component of eubacterial ribonuclease P (RNase P). In addition to the refinement and extension of known structural elements, the analyses revealed a long-range interaction that results in a second pseudoknot in the RNA.
E S, Haas, D P, Morse, J W, Brown, F J, Schmidt, N R, Pace   +4 more
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Characterization of ribonuclease P from Toxoplasma gondii

European Journal of Protistology, 1996
Summary Toxoplasma gondii ribonuclease P (RNase P) activity was identified and characterized. The enzyme cleaved the precursor of Escherichia coli tyrosine transfer RNA at a position identical to the site recognized by E. coli RNase P. The enzyme has a broad pH optimum from 7 to 9, is more active at 42°C than at 32°C and 37°C, and is relatively
D, Mack, R, McLeod, B, Stark
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