title: Ribonuclease P substrate specificity: cleavage of a bacteriophage phi80-induced RNA.
abstract: RNase P can cleave in vitro a bacteriophage phi80-induced RNA which is 62 nucleotides long [M3 RNA, G. Pieczenik et al. (1972) Arch. Biochem. Biophys. 152, 152-165] to yield two specific fragments 25 and 37 nucleotides long. As is the case for another substrate of RNase P; the precursor to Escherichia coli 4.5S RNA, the cleavage site in M3 RNA is at the end of a long double-stranded region immediately adjacent to a single-stranded segment. Similar nucleotide sequences span the cleavage site in both substrates. These and other features of the reaction of RNase P with M3 and 4.5S precursor RNA are different from some aspects of the reaction of this enzyme with tRNA precursor molecules. A qualitative scheme is presented that is directed towards the understanding of the differences in RNase P cleavage site specificity for these substrates.
mesh_terms: D001665:Binding Sites; D003090:Coliphages; D004926:Escherichia coli / Q000201:enzymology; D008954:Models, Biological; D009694:Nucleic Acid Precursors / Q000378:metabolism; D012343:RNA, Transfer / Q000096:biosynthesis; D012367:RNA, Viral / Q000378:metabolism*; D012260:Ribonucleases / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D009694:Nucleic Acid Precursors; D012367:RNA, Viral; D012343:RNA, Transfer; D012260:Ribonucleases