Thirty-three years later, a glimpse at the ribonuclease III active site.
RNase III endonucleases cleave double-stranded RNA, transforming precursor RNAs into mature RNAs that act in pre-mRNA splicing, RNA modification, translation, gene silencing, and the regulation of developmental timing. The recently solved structure of an RNase III endonuclease domain provides a hint at how this family of ribonucleases functions.
Zamore
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Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester 01655, USA.
D001665:Binding Sites; D019281:Dimerization; D004722:Endoribonucleases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins; D008274:Magnesium / Q000378:metabolism; D008954:Models, Biological; D017434:Protein Structure, Tertiary; D043244:Ribonuclease III; D013329:Structure-Activity Relationship
D029968:Escherichia coli Proteins; D004722:Endoribonucleases; D043244:Ribonuclease III; C468366:ribonuclease III, E coli; D008274:Magnesium