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 …
The yeast,Saccharomyces cerevisiae, RNase P/MRP ribonucleoprotein endoribonuclease family
TH Reilly, ME Schmitt - Molecular biology reports, 1995 - Springer
Abstract Ribonuclease P (RNase P) is a ribonucleoprotein responsible for the
endonucleolytic cleavage of the 5′-termini of tRNAs. Ribonuclease MRP (RNase MRP) is a …
endonucleolytic cleavage of the 5′-termini of tRNAs. Ribonuclease MRP (RNase MRP) is a …
RNase MRP/RNase P: a structure-function relation conserved in evolution?
R Karwan - FEBS letters, 1993 - Elsevier
Abstract RNase P and RNase MRP are related ribonucleoproteins. RNase MRP processes
mitochondrial precursor-(primer) RNAs, whereas RNase P cleaves precursor-tRNAs to …
mitochondrial precursor-(primer) RNAs, whereas RNase P cleaves precursor-tRNAs to …
A nuclear function for RNase MRP.
DA Clayton - Proceedings of the National Academy of …, 1994 - National Acad Sciences
The site-specific endoribonuclease RNase MRP was first identified 7 years ago as an RNA-
processing activity in mammalian cells (1, 2). In the original description of this …
processing activity in mammalian cells (1, 2). In the original description of this …
RNase MRP and RNase P share a common substrate
T Potuschak, W Rossmanith, R Karwan - Nucleic acids research, 1993 - academic.oup.com
RNase MRP is a site-specific ribonucleoprotein endo ribonuclease that processes RNA from
the mammalian mitochondrial displacement ioop containing region. RNase P is a site …
the mammalian mitochondrial displacement ioop containing region. RNase P is a site …
Substrate recognition by ribonucleoprotein ribonuclease MRP
O Esakova, A Perederina, C Quan, I Berezin… - Rna, 2011 - rnajournal.cshlp.org
The ribonucleoprotein complex ribonuclease (RNase) MRP is a site-specific
endoribonuclease essential for the survival of the eukaryotic cell. RNase MRP closely …
endoribonuclease essential for the survival of the eukaryotic cell. RNase MRP closely …
Characterization of human MRP/Th RNA and its nuclear gene: full length MRP/Th RNA is an active endoribonuclease when assembled as an RNP
JN Topper, DA Clayton - Nucleic acids research, 1990 - academic.oup.com
Vertebrate cells contain a site-specific endoribonuclease (RNase MRP) that cleaves
mitochondrial RNA transcribed from the origin of leading-strand mitochondrial DNA …
mitochondrial RNA transcribed from the origin of leading-strand mitochondrial DNA …
Eukaryote RNase P and RNase MRP
SC Walker, MC Marvin, DR Engelke - Ribonuclease P, 2010 - Springer
Abstract Ribonuclease P (RNase P) is an essential endonuclease that catalyzes the
cleavage of the 5′ leader sequence from precursor tRNAs (pre-tRNAs). Most forms of …
cleavage of the 5′ leader sequence from precursor tRNAs (pre-tRNAs). Most forms of …
Ribonucleoprotein ribonucleases P and MRP
AS Krasilnikov - Ribonucleases, 2011 - Springer
Abstract Ribonucleoprotein Ribonuclease (RNase) P and RNase MRP consist of a large
RNA component and an essential protein part. RNases P/MRP differ from all other known …
RNA component and an essential protein part. RNases P/MRP differ from all other known …
Structural and functional similarities between MRP and RNase P
R Reddy, S Shimba - Molecular biology reports, 1995 - Springer
RNase P, the enzyme responsible for 5′-end processing of tRNAs and 4.5 S RNA, has
been extensively characterized from E. coli. The RNA component of E. coli RNase P, without …
been extensively characterized from E. coli. The RNA component of E. coli RNase P, without …