Results 11 to 20 of about 25,923,055 (288)
Antibiotics, 2016 RNase P is an essential endonuclease in tRNA biogenesis, which generates the mature 5′-termini of tRNAs. Most forms of RNase P are ribonucleoproteins, i.e., they consist of an essential RNA and protein subunits.
Denis Drainas
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RNase P RNA-mediated catalysis
Biochemical Society Transactions, 2002 The endoribonuclease RNase P is involved in the processing of tRNA precursors to generate mature 5′ termini. The catalytic activity of RNase P is associated with an RNA, RNase P RNA. A specific interaction between the 3′ end of the substrate and RNase P RNA, to form an RNase P RNA-substrate complex, is referred to as the ‘73–294-interaction’.
Kirsebom, Leif A.,
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RNase MRP and RNase P share a common substrate
Nucleic Acids Research, 1993 RNase MRP is a site-specific ribonucleoprotein endoribonuclease that processes RNA from the mammalian mitochondrial displacement loop containing region. RNase P is a site-specific ribonucleoprotein endoribonuclease that processes pre-tRNAs to generate their mature 5'-ends.
T, Potuschak, W, Rossmanith, R, Karwan
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Solution structure of RNase P RNA [PDF]
RNA, 2011 The ribonucleoprotein enzyme ribonuclease P (RNase P) processes tRNAs by cleavage of precursor-tRNAs. RNase P is a ribozyme: The RNA component catalyzes tRNA maturation in vitro without proteins. Remarkable features of RNase P include multiple turnovers in vivo and ability to process diverse substrates.
Alexei V, Kazantsev +5 more
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RNase P — a ‘Scarlet Pimpernel’ [PDF]
Molecular Microbiology, 1995 RNase P is responsible for the maturation of the 5′‐termini of tRNA molecules in all cells studied to date. This ribonucleoprotein has to recognize and identify its cleavage site on a large number of different precursors. This review covers what is currently known about the function of the catalytic subunit of Escherichia coli RNase P, M1 RNA, and the ...
KIRSEBOM, LA,
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Coevolution of RNase P and the ribosome. [PDF]
Proc Natl Acad Sci U S ATranslation is carried out by the most conserved assemblies in biology. Among these assemblies, the ribosome and RNase P are central players. These ancient ribonucleoprotein complexes achieved structural and functional maturity by the last universal common ancestor (LUCA) of life. In prior work, we reconstructed the evolutionary history of the ribosome
Petrov AS +3 more
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RNase P Inhibitors Identified as Aggregators. [PDF]
Antimicrob Agents Chemother, 2021 RNase P is an essential enzyme responsible for tRNA 5′-end maturation. In most bacteria, the enzyme is a ribonucleoprotein consisting of a catalytic RNA subunit and a small protein cofactor termed RnpA. Several studies have reported small-molecule inhibitors directed against bacterial RNase P that were identified by high-throughput screenings.
Schencking I +8 more
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RNA Biology, 2009 Ribonuclease P (RNase P) is a ribonucleoprotein comprised of a catalytic RNA subunit and one or several protein subunits. RNase P is best known for its role in 5'-processing of tRNA precursors. RNase P enzymes from almost all forms of life, including protein-synthesizing organelles, contain an RNase P with a conserved, homologous RNA.
J Christopher, Ellis, James W, Brown
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The evolution of RNase P [PDF]
RNA, 2015 Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.050732.115. Freely available online through the RNA Open Access option.
Engelke, David R., Fierke, Carol A.
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The Bacillus subtilis RNase P holoenzyme contains two RNase P RNA and two RNase P protein subunits [PDF]
RNA, 2001 Ribonuclease P (RNase P) catalyzes the 5' maturation of precursor tRNA transcripts and, in bacteria, is composed of a catalytic RNA and a protein. We investigated the oligomerization state and the shape of the RNA alone and the holoenzyme of Bacillus subtilis RNase P in the absence of substrate by synchrotron small-angle X-ray scattering and affinity ...
X W, Fang +7 more
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