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Both N‐terminal catalytic and C‐terminal RNA binding domain contribute to substrate specificity and cleavage site selection of RNase III
Author(s) -
Conrad Christian,
Evguenieva-Hackenberg Elena,
Klug Gabriele
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03142-8
Subject(s) - endoribonuclease , rnase p , cleavage (geology) , ribonuclease iii , binding site , aquifex aeolicus , rna , biochemistry , nuclease , active site , chemistry , rhodobacter , escherichia coli , biology , enzyme , mutant , gene , paleontology , fracture (geology) , rna interference
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.