Results 21 to 30 of about 430,076 (284)
A novel experimental approach for the selective isolation and characterization of human RNase MRP
RNase MRP is a ribonucleoprotein complex involved in the endoribonucleolytic cleavage of different RNAs. Mutations in the RNA component of the RNP are the cause of cartilage hair hypoplasia.
Merel Derksen+5 more
doaj +1 more source
The evolution of RNase P [PDF]
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.
David R. Engelke, Carol A. Fierke
openaire +3 more sources
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.
James W. Brown, J. Christopher Ellis
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Conditional Expression of RNase P in the CyanobacteriumSynechocystis sp. PCC6803 Allows Detection of Precursor RNAs [PDF]
We have constructed a strain (CT1) that expresses RNase P conditionally with the aim to analyze the in vivotRNA processing pathway and the biological role that RNase P plays inSynechocystis 6803.
Cristina Tous+2 more
openalex +4 more sources
Silencing Antibiotic Resistance with Antisense Oligonucleotides
Antisense technologies consist of the utilization of oligonucleotides or oligonucleotide analogs to interfere with undesirable biological processes, commonly through inhibition of expression of selected genes.
Saumya Jani+2 more
doaj +1 more source
The Bacillus subtilis RNase P holoenzyme contains two RNase P RNA and two RNase P protein subunits [PDF]
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 ...
S. Niranjanakumari+7 more
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Is alba an RNase P subunit? [PDF]
It has been suggested that Alba, a well-established chromatin protein in Archaea, is also a subunit of the archaeal RNase P holoenzyme, based on the observation that the homolog of this protein in humans has been shown to be associated with RNase P activity.
J. Chris Ellis+2 more
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Inhibition of Eukaryotic RNase P [PDF]
Ribonuclease P (RNase P) is an essential RNA enzyme found in all phylogenetic domains that is best known for catalyzing the 5’ endonucleolytic cleavage of precursor transfer RNAs (pre-tRNAs). In bacteria, the enzyme consists of a single, catalytic RNA subunit and one small protein, while the archaeal and eukaryotic enzymes have 4-10 proteins in ...
David R. Engelke+2 more
openaire +2 more sources
The catalytic core of RNase P [PDF]
A deletion mutant of the catalytic RNA component of Escherichia coli RNase P missing residues 87-241 retains the ability to interact with the protein component to form a functional catalyst. The deletion of this phylogenetically conserved region significantly increases the Km, indicating that the deleted structures may be important for binding to the ...
Rafael Rivera-León+2 more
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A functional RNase P protein subunit of bacterial origin in some eukaryotes [PDF]
RNase P catalyzes 5′-maturation of tRNAs. While bacterial RNase P comprises an RNA catalyst and a protein cofactor, the eukaryotic (nuclear) variant contains an RNA and up to ten proteins, all unrelated to the bacterial protein.
Bernal Bayard, Pilar+5 more
core +1 more source