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The Escherichia coli endoribonuclease RNase E is essential for RNA processing and degradation. Earlier work provided evidence that RNase E exists intracellularly as part of a multicomponent complex and that one of the components of this complex is a 3'-to-5' exoribonuclease, polynucleotide phosphorylase (EC 2.7.7.8). To isolate and identify other components(More)
Escherichia coli RNase E, an essential single-stranded specific endoribonuclease, is required for both ribosomal RNA processing and the rapid degradation of mRNA. The availability of the complete sequences of a number of bacterial genomes prompted us to assess the evolutionarily conservation of bacterial RNase E. We show here that the sequence of the(More)
Three genes hemE, hemF, hemG taking part in the porphyrin biosynthesis of Bacillus subtilis were mapped by two- and tree-factor transduction crosses. The gene hemE determines uroporphyrinogen decarboxylase (EC 4.1.1.37) the gene hemF coproporyphyrinogen oxidase (EC 1.3.3.3) and the gene hemG, ferrochelatase (EC 4.99. 1.1) enzymes. The loci hemE, hemF, hemG,(More)
RNase E is a major endonucleolytic RNA processing enzyme in Escherichia coli. We have sequenced a 3.2 kb EcoRI-BamHI fragment encoding the rne gene, and identified its reading frame. Upstream from the gene, there are appropriate consensus sequences for a putative promoter and a ribosome binding site. We have translated this gene using a T7 RNA(More)
Two genes (hemB, hemC) taking part in the porphyrin biosynthesis of Bacillus subtilis were mapped. The gene hemB determines δ-aminolaevulinic acid dehydrase, and the gene hemC prophobilinogen deaminase. The transductants from the experiments were grouped by routine replica plating, and the genotypes of certain recombinant classes were determined by the(More)
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