Journal article

Publication year: 2001

Pages: 53-58

Journal: FEBS Letters

Volume number: 509

Issue number: 1

ISSN: 0014-5793

DOI Link: https://doi.org/10.1016/S0014-5793(01)03142-8

Publisher: Wiley

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. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

Harvard Citation style: 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 Letters, 509(1), pp. 53-58. https://doi.org/10.1016/S0014-5793(01)03142-8

APA Citation style: Conrad, C., Evguenieva-Hackenberg, E., & 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 Letters. 509(1), 53-58. https://doi.org/10.1016/S0014-5793(01)03142-8