Results 161 to 169 of about 56,107 (169)
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Use of RNA Secondary Structure for Studying the Evolution of RNase P and RNase MRP
Journal of Molecular Evolution, 2000Secondary structure is evaluated for determining evolutionary relationships between catalytic RNA molecules that are so distantly related they are scarcely alignable. The ribonucleoproteins RNase P (P) and RNase MRP (MRP) have been suggested to be evolutionarily related because of similarities in both function and secondary structure.
Collins, Lesley J. +2 more
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Genetic and biochemical analyses of yeast RNase MRP
Molecular Biology Reports, 1996RNase MRP cleaves the yeast pre-rRNA at a site in internal transcribed spacer 1 (ITS1) and this cleavage can be reproduced in vitro by the highly purified enzyme. Two protein components (Pop1p and Pop2p) have been identified which are common to yeast RNase MRP and RNase P.
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Structural and functional similarities between MRP and RNase P
Molecular Biology Reports, 1996RNase P, the enzyme response for 5'-end processing of tRNAs and 4.5S RNA, has been extensively characterized from E. coli. The RNA component of E. coli RNase P, without the protein, has the enzymatic activity and is the first true RNA enzyme to be characterized. RNase P and MRP are two distinct nuclear ribonucleoprotein (RNP) particles characterized in
Shigeki Shimba, Ram Reddy
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Further characterization of human RNase MRP/RNase P and related autoantibodies
Molecular Biology Reports, 1998We characterized a panel of human RNase MRP/RNase P autoantibodies by immunoprecipitation, immunodepletion, immunoaffinity purification and immunoblotting. We report on the protein spectrum that is recognized by RNase MRP/RNase P autoantibodies. We also describe another, related patient serum that based on these assays does not immunoprecipitate RNase ...
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Secondary structure of RNase MRP RNA as predicted by phylogenetic comparison.
The FASEB Journal, 1993RNase MRP is a ribonucleoprotein endoribonuclease that has been shown to cleave mitochondrial primer RNA sequences from a variety of sources. The bulk of RNase MRP activity is found in the nucleus where its function remains unknown. Two different approaches have resulted in predictions of distinct secondary structures for RNase MRP RNA.
Mark E. Schmitt +3 more
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Cryo-EM structure of catalytic ribonucleoprotein RNase MRP
, 2020Andrey S. Krasilnikov
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The Th ribonucleoprotein particle: Association with the RNA processing enzymes RNase MRP and RNase
Molecular Biology Reports, 1990P. Joe Craft, H. Gold
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