Results 21 to 30 of about 430,076 (284)

A novel experimental approach for the selective isolation and characterization of human RNase MRP

open access: yesRNA Biology, 2022
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]

open access: yesRNA, 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.
David R. Engelke, Carol A. Fierke
openaire   +3 more sources

The RNase P family [PDF]

open access: yesRNA 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.
James W. Brown, J. Christopher Ellis
openaire   +3 more sources

Conditional Expression of RNase P in the CyanobacteriumSynechocystis sp. PCC6803 Allows Detection of Precursor RNAs [PDF]

open access: hybrid, 2001
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

open access: yesBiomedicines, 2021
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]

open access: yesRNA, 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 ...
S. Niranjanakumari   +7 more
openaire   +3 more sources

Is alba an RNase P subunit? [PDF]

open access: yesRNA Biology, 2007
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
openaire   +3 more sources

Inhibition of Eukaryotic RNase P [PDF]

open access: yesBiophysical Journal, 2010
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]

open access: yesNucleic Acids Research, 1996
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
openaire   +2 more sources

A functional RNase P protein subunit of bacterial origin in some eukaryotes [PDF]

open access: yes, 2011
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

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