A cleavage site of ribonuclease F. A putative processing endoribonuclease from Escherichia coli

Eur J Biochem. 1982 Jun;124(3):553-9.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Base Sequence
  • Binding Sites
  • Coliphages / enzymology
  • Endoribonucleases*
  • Escherichia coli / enzymology*
  • Hot Temperature
  • Oligonucleotides / metabolism
  • RNA, Bacterial / metabolism*
  • Ribonucleases / metabolism*

Substances

  • Oligonucleotides
  • RNA, Bacterial
  • Endoribonucleases
  • Ribonucleases
  • ribonuclease F