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. 1991 Jan 1;88(1):1–5. doi: 10.1073/pnas.88.1.1

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

P Babitzke 1, S R Kushner 1
PMCID: PMC50735  PMID: 1846032

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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