RNase MRP/RNase P: a structure-function relation conserved in evolution?
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. All known RNase P and RNase MRP RNAs contain conserved structural elements possibly involved in catalysis/substrate binding, but these elements do not predict all cellular functions of the RNPs.
Karwan
R
R
Institute of Tumor Biology, University of Vienna, Austria.
D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D017124:Conserved Sequence; D004722:Endoribonucleases / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D012313:RNA / Q000378:metabolism; D016337:RNA, Catalytic / Q000737:chemistry / Q000378:metabolism; D043262:Ribonuclease P; D013329:Structure-Activity Relationship
D016337:RNA, Catalytic; D012313:RNA; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; C468368:RPP14 protein, human; D043262:Ribonuclease P