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Ribonuclease P substrate specificity: cleavage of a bacteriophage phi80-induced RNA.
Author(s) -
Alfred L.M. Bothwell,
Benjamin C. Stark,
Sidney Altman
Publication year - 1976
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.73.6.1912
Subject(s) - rnase p , rna , cleavage (geology) , nucleotide , ribonuclease , rnase h , transfer rna , degradosome , ribonuclease iii , microbiology and biotechnology , biology , escherichia coli , cleave , biochemistry , chemistry , enzyme , gene , paleontology , fracture (geology) , rna interference
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.

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