Abstract
The in vitro and in vivo analysis of the ribonuclease E-deficient (rne-) and the altered mRNA stability protein-deficient (ams-) strains of Escherichia coli has demonstrated that they carry mutations in the same structural gene. Strains encoding either thermolabile RNase E (rne-3071) or Ams protein (ams-1) are defective in both rRNA processing and mRNA turnover. Immediately after a shift to the nonpermissive temperature, the chemical decay rate of bulk mRNA is slowed 2- to 3-fold, and within 70 min, precursors to 5S rRNA begin to accumulate. In addition, all of the phenotypes associated with either the rne-3071 or the ams-1 alleles were complemented by a recombinant plasmid carrying ams+. When taken together with previous genetic studies, these results suggest that the role of ribonuclease E in mRNA turnover involves endonucleolytic cleavages at the proposed ACAG(A/U)AUUUG consensus sequence.
MeSH Terms
Bacterial Proteins/genetics,metabolism
Base Sequence
Chromosome Deletion
DNA Transposable Elements
Endoribonucleases/genetics,metabolism
Escherichia coli/enzymology,genetics
Genes, Bacterial
Genetic Complementation Test
Genotype
Kinetics
Molecular Sequence Data
Operon
RNA, Messenger/metabolism
Chemicals
Bacterial Proteins
DNA Transposable Elements
RNA, Messenger
Endoribonucleases
ribonuclease E
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Babitzke P
Department of Genetics, University of Georgia, Athens 30602.
Kushner S R
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