Both N-terminal catalytic and C-terminal RNA binding domain contribute to substrate specificity and cleavage site selection of RNase III

FEBS Lett. 2001 Nov 30;509(1):53-8. doi: 10.1016/s0014-5793(01)03142-8.


The double-stranded RNA-specific endoribonuclease III (RNase III) of bacteria consists of an N-terminal nuclease domain and a double-stranded RNA binding domain (dsRBD) at the C-terminus. Analysis of two hybrid proteins consisting of the N-terminal half of Escherichia coli RNase III fused to the dsRBD of the Rhodobacter capsulatus enzyme and vice versa reveals that both domains in combination with the particular substrate determine substrate specificity and cleavage site selection. Extension of the spacer between the two domains of the E. coli enzyme from nine to 20 amino acids did not affect cleavage site selection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Binding Sites
  • Catalytic Domain
  • Cloning, Molecular
  • DNA / metabolism
  • Endoribonucleases / metabolism*
  • Escherichia coli / metabolism
  • Escherichia coli Proteins*
  • Molecular Sequence Data
  • Plasmids / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA / metabolism*
  • RNA, Double-Stranded / metabolism
  • Recombinant Fusion Proteins / metabolism
  • Ribonuclease III
  • Substrate Specificity
  • Transcription, Genetic
  • Yeasts / metabolism


  • Escherichia coli Proteins
  • RNA, Double-Stranded
  • Recombinant Fusion Proteins
  • RNA
  • DNA
  • Endoribonucleases
  • Ribonuclease III
  • ribonuclease III, E coli