A cleavage site of ribonuclease F. A putative processing endoribonuclease from Escherichia coli.
A new endoribonuclease activity, RNase F, was partially purified from Escherichia coli cells. This activity can specifically cleave a precursor RNA molecule (of species 1) isolated from T4-infected cells [N. Watson & D. Apirion (1981) Biochem. Biophys. Res. Commun. 103, 543-551]. The cleavage results in products which are very similar to RNA molecules found in the cell, generating a 3'-phosphate and a 5'-hydroxyl groups. The cleavage takes place between a cytosine and an adenine moiety, within a possible loop and stem structure; the cut is in the border between the double-stranded and single-stranded regions of this structure. This specificity of this enzyme could be the introduction of a cleavage near the 3' ends of tRNA molecules and other RNAs like species 1 which could resemble tRNA in their three-dimensional structure.
D001483:Base Sequence; D001665:Binding Sites; D003090:Coliphages / Q000201:enzymology; D004722:Endoribonucleases; D004926:Escherichia coli / Q000201:enzymology*; D006358:Hot Temperature; D009841:Oligonucleotides / Q000378:metabolism; D012329:RNA, Bacterial / Q000378:metabolism*; D012260:Ribonucleases / Q000378:metabolism*
D009841:Oligonucleotides; D012329:RNA, Bacterial; D004722:Endoribonucleases; D012260:Ribonucleases; C021885:ribonuclease F