Differential degradation of theEscherichia colipolynucleotide phosphorylase mRNA
Open Access
- 1 January 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 17 (18) , 7441-7451
- https://doi.org/10.1093/nar/17.18.7441
Abstract
The transcript covering pnp, the gene encoding polynucleotide phosphorylase, is processed by RNaseIII at the 5′-upstream site of the pnp gene. In the RNaseIII-deficient strain, three species of the unprocessed transcript with different lengths could be detected. In this study, the stability of each transcript was analyzed by SI nuclease protection assay. The results show that the half-lives of the unprocessed transcripts are 8 min, whereas the half-life of the processed transcript is 1.5 min. It is also shown that the 5′ segment of the unprocessed transcripts is more stable than the middle or the 3′ segment.This publication has 20 references indexed in Scilit:
- Mechanisms of mRNA decay in bacteria: a perspectiveGene, 1988
- Site-specific endonucleolytic cleavages and the regulation of stability of E. coli ompA mRNACell, 1988
- Processed mRNA with differential stability in the regulation of E. coli pilin gene expressionCell, 1988
- Differential mRNA stability controls relative gene expression within a polycistronic operonCell, 1987
- Initiation, attenuation and RNase III processing of transcripts from the Escherichia coli operon encoding ribosomal protein S15 and polynucleotide phosphorylaseJournal of Molecular Biology, 1986
- Nucleotide sequence of the gene for Escherichia coli ribosomal protein S15 (rpsO)Molecular Genetics and Genomics, 1984
- Growth-rate dependent regulation of mRNA stability in Escherichia coliNature, 1984
- mRNA processing inEscherichia coli: an activity encoded by the host processes bacteriophage f1 mRNAsNucleic Acids Research, 1984
- The operen that encodes the sigma subunit of RNA polymerase also encodes ribosomal protein S21 and DNA primase in E. coli K12Cell, 1983
- In vitro Synthesis of Bacteriophage LysozymeNature, 1967