Ribonuclease P substrate specificity: cleavage of a bacteriophage phi80-induced RNA
- PMID: 778851
- PMCID: PMC430417
- DOI: 10.1073/pnas.73.6.1912
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.
Similar articles
-
Transfer ribonucleic acid biosynthesis. Substrate specificity of ribonuclease P.J Biol Chem. 1976 Apr 25;251(8):2440-5. J Biol Chem. 1976. PMID: 770465
-
A mutant of escherichia coli defective in removing 3' terminal nucleotides from some transfer RNA precursor molecules.Cell. 1975 Aug;5(4):389-400. doi: 10.1016/0092-8674(75)90058-6. Cell. 1975. PMID: 1098779
-
A cleavage site of ribonuclease F. A putative processing endoribonuclease from Escherichia coli.Eur J Biochem. 1982 Jun;124(3):553-9. Eur J Biochem. 1982. PMID: 6179777
-
Sequential processing of precursor tRNA molecules in Escherichia coli.Proc Natl Acad Sci U S A. 1975 Sep;72(9):3369-73. doi: 10.1073/pnas.72.9.3369. Proc Natl Acad Sci U S A. 1975. PMID: 1103144 Free PMC article.
-
Transcription and processing of transfer RNA precursors.Prog Nucleic Acid Res Mol Biol. 1976;16:25-73. doi: 10.1016/s0079-6603(08)60755-2. Prog Nucleic Acid Res Mol Biol. 1976. PMID: 766079 Review. No abstract available.
Cited by
-
Substrate recognition by RNase P and by the catalytic M1 RNA: identification of possible contact points in pre-tRNAs.EMBO J. 1990 Jun;9(6):1929-37. doi: 10.1002/j.1460-2075.1990.tb08320.x. EMBO J. 1990. PMID: 2347311 Free PMC article.
-
Rpp1, an essential protein subunit of nuclear RNase P required for processing of precursor tRNA and 35S precursor rRNA in Saccharomyces cerevisiae.Genes Dev. 1997 Sep 15;11(18):2414-25. doi: 10.1101/gad.11.18.2414. Genes Dev. 1997. Corrected and republished in: Genes Dev. 1997 Nov 1;11(21):2926-37. doi: 10.1101/gad.11.21.2926. PMID: 9308968 Free PMC article. Corrected and republished.
-
Properties of a monovalent and divalent requiring endoribonuclease with novel specificity from calf heart.Nucleic Acids Res. 1983 Jun 11;11(11):3687-702. doi: 10.1093/nar/11.11.3687. Nucleic Acids Res. 1983. PMID: 6406982 Free PMC article.
-
Structural features of Bacillus precursor 5S RNA involved in the interaction with RNAase M5.Nucleic Acids Res. 1980 Nov 25;8(22):5411-21. doi: 10.1093/nar/8.22.5411. Nucleic Acids Res. 1980. PMID: 6162151 Free PMC article.
-
Multiple binding modes of substrate to the catalytic RNA subunit of RNase P from Escherichia coli.RNA. 1999 Aug;5(8):1021-33. doi: 10.1017/s1355838299990416. RNA. 1999. PMID: 10445877 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials