Back to Search Start Over

Ribonuclease P substrate specificity: cleavage of a bacteriophage phi80-induced RNA.

Authors :
Bothwell, A L
Stark, B C
Altman, S
Source :
Proceedings of the National Academy of Sciences of the United States of America; June 1976, Vol. 73 Issue: 6 p1912-1916, 5p
Publication Year :
1976

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.

Details

Language :
English
ISSN :
00278424 and 10916490
Volume :
73
Issue :
6
Database :
Supplemental Index
Journal :
Proceedings of the National Academy of Sciences of the United States of America
Publication Type :
Periodical
Accession number :
ejs60427455
Full Text :
https://doi.org/10.1073/pnas.73.6.1912