RNase MRP Cleaves Pre-tRNASer-Met in the tRNA Maturation Pathway
Y Saito, J Takeda, K Adachi, Y Nobe, J Kobayashi… - PLoS …, 2014 - journals.plos.org
Ribonuclease mitochondrial RNA processing (RNase MRP) is a multifunctional
ribonucleoprotein (RNP) complex that is involved in the maturation of various types of RNA …
ribonucleoprotein (RNP) complex that is involved in the maturation of various types of RNA …
A functional dominant mutation in Schizosaccharomyces pombe RNase MRP RNA affects nuclear RNA processing and requires the mitochondrial‐associated nuclear …
JL Paluh, DA Clayton - The EMBO Journal, 1996 - embopress.org
The essential gene for RNase MRP RNA, mrp1, was identified previously in
Schizosaccharomyces pombe by homology to mammalian RNase MRP RNAs. Here we …
Schizosaccharomyces pombe by homology to mammalian RNase MRP RNAs. Here we …
Coevolution of RNA and protein subunits in RNase P and RNase MRP, two RNA processing enzymes
B Zhou, F Wan, KX Lei, P Lan, J Wu, M Lei - Journal of Biological Chemistry, 2024 - ASBMB
RNase P and RNase mitochondrial RNA processing (MRP) are ribonucleoproteins (RNPs)
that consist of a catalytic RNA and a varying number of protein cofactors. RNase P is …
that consist of a catalytic RNA and a varying number of protein cofactors. RNase P is …
Interplay between substrate recognition, 5′ end tRNA processing and methylation activity of human mitochondrial RNase P
Human mitochondrial ribonuclease P (mtRNase P) is an essential three-protein complex
that catalyzes the 5′ end maturation of mitochondrial precursor tRNAs (pre-tRNAs) …
that catalyzes the 5′ end maturation of mitochondrial precursor tRNAs (pre-tRNAs) …
Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component
K Salinas, S Wierzbicki, L Zhou, ME Schmitt - Journal of Biological …, 2005 - ASBMB
In the yeast Saccharomyces cerevisiae, RNase mitochondrial RNA processing (MRP) is an
essential endoribonuclease that consists of one RNA component and at least nine protein …
essential endoribonuclease that consists of one RNA component and at least nine protein …
Structural basis of RNA processing by human mitochondrial RNase P
Human mitochondrial transcripts contain messenger and ribosomal RNAs flanked by
transfer RNAs (tRNAs), which are excised by mitochondrial RNase (mtRNase) P and Z to …
transfer RNAs (tRNAs), which are excised by mitochondrial RNase (mtRNase) P and Z to …
Probing the structure of Saccharomyces cerevisiae RNase MRP
SC Walker, TV Aspinall, JMB Gordon, JM Avis - 2005 - portlandpress.com
In yeast, RNase MRP (mitochondrial RNA processing), a ribonucleoprotein precursor rRNA
processing enzyme, possesses one putatively catalytic RNA and ten protein subunits and is …
processing enzyme, possesses one putatively catalytic RNA and ten protein subunits and is …
Characterization of ribonuclease MRP function
T Cai, ME Schmitt - Methods in enzymology, 2001 - Elsevier
Publisher Summary Ribonuclease (RNase) MRP is a ribonucleoprotein endoribonuclease
that cleaves an RNA sequence in a site-specific manner. The enzyme has two known RNA …
that cleaves an RNA sequence in a site-specific manner. The enzyme has two known RNA …
Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components
Q Lu, S Wierzbicki, AS Krasilnikov, ME Schmitt - RNA, 2010 - rnajournal.cshlp.org
RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm …
[HTML][HTML] Subtle determinants of the nucleocytoplasmic partitioning of in vivo-transcribed RNase MRP RNA in Xenopus laevis oocytes
S Jeong-Yu, AF Davis, DA Clayton - Gene Expression, 1996 - ncbi.nlm.nih.gov
RNase MRP is a ribonucleoprotein originally identified on the basis of its ability to cleave
RNA endonucleolytically from origins of mitochondrial DNA replication, rendering it a likely …
RNA endonucleolytically from origins of mitochondrial DNA replication, rendering it a likely …