The ams (altered mRNA stability) protein and ribonuclease E are encoded by the same structural gene of Escherichia coli

P. Babitzke, S. R. Kushner

Research output: Contribution to journalArticle

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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.

Original languageEnglish (US)
Pages (from-to)1-5
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number1
DOIs
StatePublished - 1991

All Science Journal Classification (ASJC) codes

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