Results 51 to 60 of about 18,946,844 (347)
RNase P Branches Out from RNP to Protein: Organelle-Triggered Diversification? [PDF]
, 2012 RNase P is the enzyme that removes 5′ leader sequences from precursor tRNAs. Remarkably, in most organisms, RNase P is a ribonucleoprotein particle where the RNA component is responsible for catalysis. In this issue of Genes \u26 Development, Gutmann and
Borah, Sumit +2 more
core +3 more sources
Stability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP
Nature Communications, 2020 RNase P and MRP are highly conserved, multi-protein/RNA complexes with essential roles in processing ribosomal and tRNAs. Three proteins found in both complexes, Pop1, Pop6, and Pop7 are also telomerase-associated.
P. Garcia +7 more
semanticscholar +1 more source
Evolution of ribonuclease H genes in prokaryotes to avoid inheritance of redundant genes
BMC Evolutionary Biology, 2007 Background A theoretical model of genetic redundancy has proposed that the fates of redundant genes depend on the degree of functional redundancy, and that functionally redundant genes will not be inherited together.
Tomita Masaru +2 more
doaj +1 more source
Genetic diversity of human RNase 8
BMC Genomics, 2012 Background Ribonuclease 8 is a member of the RNase A family of secretory ribonucleases; orthologs of this gene have been found only in primate genomes. RNase 8 is a divergent paralog of RNase 7, which is lysine-enriched, highly conserved, has prominent ...
Chan Calvin C +4 more
doaj +1 more source
P finder: genomic and metagenomic annotation of RNase P RNA gene (rnpB)
BMC Genomics, 2020 Background The rnpB gene encodes for an essential catalytic RNA (RNase P). Like other essential RNAs, RNase P’s sequence is highly variable. However, unlike other essential RNAs (i.e.
J. Christopher Ellis
doaj +1 more source
Nucleic Acids Research, 2020 Ribonuclease P (RNase P) is essential for the 5′-end maturation of tRNAs in all kingdoms of life. In Escherichia coli, temperature sensitive mutations in either its protein (rnpA49) and or RNA (rnpB709) subunits lead to inviability at nonpermissive ...
B. K. Mohanty +2 more
semanticscholar +1 more source
Insights into the structure and activity of prototype foamy virus RNase H
Retrovirology, 2012 Background RNase H is an endonuclease that hydrolyzes the RNA strand in RNA/DNA hybrids. Retroviral reverse transcriptases harbor a C-terminal RNase H domain whose activity is essential for viral replication.
Leo Berit +4 more
doaj +1 more source
Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP
Nature Communications, 2020 Ribozyme-based RNase MRP is an essential eukaryotic enzyme involved in the maturation of rRNA and is evolutionarily related to RNase P. Here, the authors present the 3.0 Å cryo-EM structure of the S.
Anna Perederina +6 more
doaj +1 more source
Influence of Conformation of M. tuberculosis RNase P Protein Subunit on Its Function. [PDF]
PLoS ONE, 2016 RNase P is an essential enzyme that processes 5' end leader sequence of pre-tRNA to generate mature tRNA. The bacterial RNase Ps contain a RNA subunit and one protein subunit, where the RNA subunit contains the catalytic activity.
Alla Singh +3 more
doaj +1 more source
Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins
BMC Evolutionary Biology, 2010 Background The unfolding speed of some hyperthermophilic proteins is dramatically lower than that of their mesostable homologs. Ribonuclease HII from the hyperthermophilic archaeon Thermococcus kodakaraensis (Tk-RNase HII) is stabilized by its remarkably
Koga Yuichi +8 more
doaj +1 more source