Results 11 to 20 of about 20,593,893 (291)
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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Towards plant resistance to viruses using protein-only RNase P [PDF]
Nature Communications, 2021 New approaches to plant disease control are important for pathogens that are difficult to control by existing methods. Here, the authors report a potential strategy to combat plant viruses by cytosolic expressed protein-only RNase P and show its ability ...
Anthony Gobert +8 more
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RNase MRP/RNase P: a structure-function relation conserved in evolution? [PDF]
FEBS Letters, 1993 RNase P and RNase MRP are related ribonucleoproteins. RNase MRP processes mitochondrial precursor‐ (primer) RNAs, whereas RNase P cleaves precursor‐tRNAs to produce their mature 5'‐ends. Both RNase P and RNase MRP are associated with the Th/To ribonucleoprotein suggesting possible interrelated pathways and/or functions.
Robert Karwan, Karwan, Robert
exaly +5 more sources
Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P [PDF]
RNA Biology, 2023 RNA-based enzyme RNase P is a ribonucleoprotein complex responsible primarily for 5’-maturation of tRNAs. S. cerevisiae RNase P comprises a catalytic RNA component and nine proteins. The assembly and maturation of S.
Anna Perederina +2 more
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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
europepmc +4 more sources
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
openaire +4 more sources
An RNA ligase partner for the prokaryotic protein-only RNase P: insights into the functional diversity of RNase P from genome mining [PDF]
mBioRNase P can use either an RNA- or a protein-based active site to catalyze 5′-maturation of transfer RNAs (tRNAs). This distinctive attribute in the biocatalytic repertoire raises questions about the underlying evolutionary driving forces, especially if ...
Rekha Seshadri, Venkat Gopalan
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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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Structure and mechanistic features of the prokaryotic minimal RNase P [PDF]
eLife, 2021 Endonucleolytic removal of 5’-leader sequences from tRNA precursor transcripts (pre-tRNAs) by ribonuclease P (RNase P) is essential for protein synthesis.
Rebecca Feyh +7 more
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Engineering of RNase P Ribozymes for Therapy against Human Cytomegalovirus Infection [PDF]
VirusesNucleic acid-based gene interference and editing strategies, such as antisense oligonucleotides, ribozymes, RNA interference (RNAi), and CRISPR/Cas9 coupled with guide RNAs, are exciting research tools and show great promise for clinical applications in ...
Adam Smith +3 more
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