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

FEBS Letters

Klug, Gabriele¹  Evguenieva-Hackenberg, Elena¹  Conrad, Christian¹ 

[1] Institut für Mikro- und Molekularbiologie der Justus-Liebig-Universität Giessen, Heinrich-Buff-Ring 26–32, 35392 Giessen, Germany

关键词: RNase III;    Double-stranded RNA binding domain;    Hybrid protein;    RNA processing;    Rhodobacter;    dsRNA;    double-stranded RNA;    dsRBD;    double-stranded RNA binding domain;   

DOI  :  10.1016/S0014-5793(01)03142-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown