Abstract
Human cells have the remarkable capability to regulate protein production by degrading target mRNA by two pathways: RNA interference (RNAi) and micro RNA (miRNA). Central to these pathways is the protein Argonaute‐2 (Ago‐2). In the RNAi pathway, small RNAs derived from viruses are used by Ago‐2 to slice virus mRNA, protecting the cells from infection. In the miRNA pathway, Ago‐2 utilizes naturally occurring miRNA to slice cellular mRNAs to control protein production. Ago‐2 works by binding small (~22 nucleotide) regulatory RNAs (siRNA and miRNA) to target mRNA by base pairing. Ago‐2 attaches to the phosphate backbone of the regulatory RNA, that guides Ago‐2 to the target RNA. The RNase domain of Ago‐2 (containing His807, Asp669, Asp597, and Glu637 in its active site) then “slices” the target to initiate degradation. Scientists can reduce the level of disease‐causing proteins (for example, in breast cancer) using the siRNA pathway. Determining the structure of Ago‐2 allowed researchers to understand how this enzyme functions in the siRNA/miRNA pathways. The Brown Deer High School SMART (Students Modeling A Research Topic) Team has designed a model of Ago‐2 using 3D printing technology to investigate its structure‐function relationship. SMART Team programs are supported by a grant from NIH‐CTSA.
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