Article
Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage.
Structure (London, England : 1993) - 1 Dec 2001
Blaszczyk J, Tropea J E, Bubunenko M, Routzahn K M, Waugh D S, Court D L, Ji X
Abstract excerpt
BACKGROUND: Aquifex aeolicus Ribonuclease III (Aa-RNase III) belongs to the family of Mg(2+)-dependent endonucleases that show specificity for double-stranded RNA (dsRNA). RNase III is conserved in all known bacteria and eukaryotes and has 1-2 copies of a 9-residue consensus sequence, known as the RNase III signature motif. The bacterial RNase III proteins are the simplest, consisting of two domains: an...
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