A multiple mutant of Escherichia coli lacking the exoribonucleases RNase II, RNase D, and RNase BN.
A multiple mutant strain of Escherichia coli containing mutations affecting the exoribonucleases, RNase II, RNase D, and RNase BN, and also the endonuclease, RNase I, was constructed by P1-mediated transduction. Extracts of the mutant strain were lacking the aforementioned RNase activities. The multiple mutant displayed normal growth in both rich and minimal media at a variety of temperatures, recovered from starvation essentially as the wild-type parent, and could support the growth of a variety of bacteriophages. In addition, RNA synthesis was normal and no precursor RNA accumulation was observed. The properties of the mutant strain indicate that the three exoribonucleases are not essential for the viability of E. coli. The implications of these findings to our understanding of RNA processing and degradation are discussed.
D004722:Endoribonucleases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D029968:Escherichia coli Proteins; D005095:Exoribonucleases / Q000378:metabolism*; D009154:Mutation; D012313:RNA / Q000096:biosynthesis; D043244:Ribonuclease III; D013604:T-Phages / Q000378:metabolism
D029968:Escherichia coli Proteins; D012313:RNA; D004722:Endoribonucleases; D005095:Exoribonucleases; C038206:ribonuclease BN; C022535:exoribonuclease II; D043244:Ribonuclease III; C468366:ribonuclease III, E coli