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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.
Sylvia C. Darr +2 more
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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.
Roland K. Hartmann, Enno Hartmann
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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 ...
Jeffrey C. Kurz, Carol A. Fierke
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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.
Nayef Jarrous, Sidney 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.
Nayef Jarrous, Sidney Altman
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Modifications of ribonuclease A induced by p-benzoquinone
Bioorganic Chemistry, 2012The nature of ribonuclease A (RNase) modifications induced by p-benzoquinone (pBQ) was investigated using several analysis methods. SDS-PAGE experiments revealed that pBQ was efficient in producing oligomers and polymeric aggregates when RNase was incubated with pBQ.
Albert R. Vaughn +4 more
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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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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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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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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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