Enzyme’s structure helped elucidate RNAi’s mechanism

Ten years ago, researchers obtained the first crystal structure of Dicer, a key enzyme in a biological process called RNA interference (RNAi). In RNAi, a process also known as gene silencing, a short RNA binds to mRNA, preventing mRNA’s sequence from being transcribed into a protein. The determination of Dicer’s structure by Jennifer A. Doudna of the University of California, Berkeley, and coworkers helped confirm how the enzyme processes RNA and thus advanced RNAi technology (Science 2006, DOI: 10.1126/science.1121638). More recently, Doudna and coworkers also helped discover CRISPR-Cas9, a technology with broader gene-editing applications. RNAi was discovered about 20 years ago by Andrew Z. Fire and Craig C. Mello when they were researchers at the Carnegie Institution of Washington. Fire and Mello won a 2006 Nobel Prize for this work because it revealed RNAi to be a previously unknown mechanism for gene regulation and opened up the potential for a