PMID:11734205

Citation	Conrad, C, Evguenieva-Hackenberg, E and Klug, G (2001) Both N-terminal catalytic and C-terminal RNA binding domain contribute to substrate specificity and cleavage site selection of RNase III. FEBS Lett. 509:53-8
Abstract	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.
Links	PubMed
Keywords	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
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