Results 1 to 10 of about 461,493 (219)
Antisense inhibition of bacterial RNase P [PDF]
Ziel der vorliegenden Arbeit war die in vitro- und in vivo-Inhibition bakterieller RNase P mit Antisense-Oligonukleotiden (AS-ON). RNase P ist ein essentielles Ribonukleoproteinenzym, das in allen drei Reichen des Lebens für die Reifung der ptRNAs ...
Heike Grügelsiepe
core +6 more sources
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
doaj +3 more sources
Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P [PDF]
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
doaj +2 more sources
Function and assembly of a chromatin-associated RNase P that is required for efficient transcription by RNA polymerase I. [PDF]
Human RNase P has been initially described as a tRNA processing enzyme, consisting of H1 RNA and at least ten distinct protein subunits. Recent findings, however, indicate that this catalytic ribonucleoprotein is also required for transcription of small ...
Robert Reiner +3 more
doaj +3 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]
RNase 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
doaj +2 more sources
RNase P Inhibitors Identified as Aggregators. [PDF]
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
europepmc +4 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 ...
Cameron Green
openalex +3 more sources
A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme [PDF]
RNase P, an RNA-protein complex, is essential for processing tRNAs. Three of the ten protein subunits of Saccharomyces cerevisiae RNase P (and a related complex, RNase MRP) co-purify with yeast telomerase, another RNA-protein complex.
P. Daniela Garcia, Virginia A. Zakian
doaj +2 more sources
RNase MRP/RNase P: a structure‐function relation conserved in evolution? [PDF]
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
openalex +4 more sources
Structure and mechanistic features of the prokaryotic minimal RNase P [PDF]
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
doaj +2 more sources

