作者: P. Babitzke , S. R. Kushner
DOI: 10.1073/PNAS.88.1.1
关键词: Structural gene 、 Thermolabile 、 RRNA processing 、 Molecular biology 、 Operon 、 Escherichia coli 、 Ribonuclease 、 Ribonuclease E 、 RNase P 、 Biology
摘要: Abstract The in vitro and vivo analysis of the ribonuclease E-deficient (rne-) altered mRNA stability protein-deficient (ams-) strains Escherichia coli has demonstrated that they carry mutations same structural gene. Strains encoding either thermolabile RNase E (rne-3071) or Ams protein (ams-1) are defective both rRNA processing turnover. Immediately after a shift to nonpermissive temperature, chemical decay rate bulk is slowed 2- 3-fold, within 70 min, precursors 5S begin accumulate. In addition, all phenotypes associated with rne-3071 ams-1 alleles were complemented by recombinant plasmid carrying ams+. When taken together previous genetic studies, these results suggest role turnover involves endonucleolytic cleavages at proposed ACAG(A/U)AUUUG consensus sequence.