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Folding of a universal ribozyme: the ribonuclease P RNA
Quarterly Reviews of Biophysics, 2007AbstractRibonuclease P is among the first ribozymes discovered, and is the only ubiquitously occurring ribozyme besides the ribosome. The bacterial RNase P RNA is catalytically active without its protein subunit and has been studied for over two decades as a model system for RNA catalysis, structure and folding. This review focuses on the thermodynamic,
Tobin R. Sosnick +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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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.
Reza Salavati +2 more
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Purification and characterization of potato ribonuclease P
Journal of Plant Biochemistry and Biotechnology, 2012Ribonuclease P (RNase P), a ribonucleo-protein endoribonuclease, responsible for 5′ maturation of precursor tDNA, is well characterized in bacteria, yeast and human, but not in plant. Attempt has been made to partially purify and characterize nuclear RNase P from potato.
Duni Chand +2 more
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Structures of eukaryotic ribonuclease P
Science, 2018Structural Biology Ribonuclease P (RNase P) is a ribozyme that processes transfer RNA (tRNA) precursors and is found in all three kingdoms of life. Now, Lan et al. report the structures of yeast RNase P (see the Perspective by Scott and Nagai).
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2009
Two gene-targeting approaches have been developed with the use of RNase P. The first approach is based on an external guide sequence (EGS), which consists of a sequence complementary to a target mRNA and, when noncovalently complexed with RNase P, renders the target RNA susceptible to degradation by the ribonuclease.
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Two gene-targeting approaches have been developed with the use of RNase P. The first approach is based on an external guide sequence (EGS), which consists of a sequence complementary to a target mRNA and, when noncovalently complexed with RNase P, renders the target RNA susceptible to degradation by the ribonuclease.
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Crystal structure of the specificity domain of ribonuclease P
Nature, 2003RNase P is the only endonuclease responsible for processing the 5' end of transfer RNA by cleaving a precursor and leading to tRNA maturation. It contains an RNA component and a protein component and has been identified in all organisms. It was one of the first catalytic RNAs identified and the first that acts as a multiple-turnover enzyme in vivo ...
Andrey S. Krasilnikov +3 more
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A Structural Analysis of Ribonuclease P
2007The endonucleolytic cleavage of precursor sequences from the 5′-end of transfer RNA (tRNA) precursors to form the mature 5′-end is catalyzed by a remarkably complex and unusual enzyme, ribonuclease P (RNase P)(Figure 9.1).1–4 RNase P is ubiquitous, found in cells from all three domains of life: Bact...
Norman R. Pace +3 more
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Long-Range Structure in Ribonuclease P RNA
Science, 1991Phylogenetic-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.
James W. Brown +4 more
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Characterization of ribonuclease P from Toxoplasma gondii
European Journal of Protistology, 1996Summary 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
Douglas G. Mack +4 more
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