RNase III cleavage of Escherichia coli beta-galactosidase and tryptophan operon mRNA.
Purified RNase III of Escherichia coli cleaved the initial 479-nucleotide sequence of lac operon mRNA at four specific sites and also gave limited cleavage of trp operon mRNA. This action explains the inactivation of mRNA coding capacity by RNase III in vitro.
D001483:Base Sequence; D004720:Endonucleases / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D007763:Lac Operon; D009876:Operon; D012329:RNA, Bacterial / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D043244:Ribonuclease III; D012260:Ribonucleases / Q000378:metabolism*; D014364:Tryptophan / Q000096:biosynthesis; D001616:beta-Galactosidase / Q000235:genetics
D029968:Escherichia coli Proteins; D012329:RNA, Bacterial; D012333:RNA, Messenger; D014364:Tryptophan; D004720:Endonucleases; D012260:Ribonucleases; D043244:Ribonuclease III; C468366:ribonuclease III, E coli; D001616:beta-Galactosidase