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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.
James W. Brown, Norman R. Pace
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1988
Ribonuclease P is an enzyme that cleaves tRNA precursors to generate the 5’ termini of mature tRNA sequences. In E. coli this enzyme consists of a catalytic RNA subunit and a protein cofactor. In the absence of direct cloning of the gene for the RNA component and functional assays of the transcript of that cloned gene, it is possible to perform other ...
Sidney Altman +2 more
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Ribonuclease P is an enzyme that cleaves tRNA precursors to generate the 5’ termini of mature tRNA sequences. In E. coli this enzyme consists of a catalytic RNA subunit and a protein cofactor. In the absence of direct cloning of the gene for the RNA component and functional assays of the transcript of that cloned gene, it is possible to perform other ...
Sidney Altman +2 more
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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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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.
James W. Brown, Elizabeth S. Haas
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Structure of ribonuclease P — a universal ribozyme
Current Opinion in Structural Biology, 2006Ribonuclease P (RNase P) is one of only two known universal ribozymes and was one of the first ribozymes to be discovered. It is involved in RNA processing, in particular the 5' maturation of tRNA. Unlike most other natural ribozymes, it recognizes and cleaves its substrate in trans. RNase P is a ribonucleoprotein complex containing one RNA subunit and
Alfredo Torres-Larios +3 more
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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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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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Properties of purified ribonuclease P from Escherichia coli.
Biochemistry, 1981The purified protein moiety of ribonuclease P (EC 3.1.26.5) from Escherichia coli, a single polypeptide of molecular weight approximately 17 500, has not catalytic activity by itself on several RNA substrates.
R. Kole, S. Altman
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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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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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