Genetic and biochemical analyses of yeast RNase MRP.
RNase 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. Moreover, purified RNase P can also cleave the pre-rRNA substrate in vitro, underlining the similarities between these particles. Genetic evidence suggests that RNase MRP functionally interacts with the snoRNPs which are required for other pre-RNA processing reactions.
Tollervey
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European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
D004275:DNA, Ribosomal / Q000737:chemistry / Q000378:metabolism*; D004722:Endoribonucleases / Q000737:chemistry / Q000378:metabolism*; D012322:RNA Precursors / Q000378:metabolism; D016337:RNA, Catalytic / Q000737:chemistry / Q000378:metabolism; D012331:RNA, Fungal / Q000378:metabolism; D012335:RNA, Ribosomal / Q000096:biosynthesis; D043262:Ribonuclease P; D017411:Ribonucleoproteins, Small Nuclear / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*
D004275:DNA, Ribosomal; D012322:RNA Precursors; D016337:RNA, Catalytic; D012331:RNA, Fungal; D012335:RNA, Ribosomal; D017411:Ribonucleoproteins, Small Nuclear; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; D043262:Ribonuclease P