The three-dimensional structure of one of the most important molecular players in RNA interference (RNAi), the protein Argonaute-2, has just been resolved by investigators at the Cold Spring Harbor Laboratory (CSHL).
This study is very important, and could have far-reaching ramifications for molecular biology, primarily because RNA interference is a mechanism involved in a massive number of biological processes. The latter include the development patterns each organism takes to grow.
Argonaute-2 is bound to ribonucleic acid because the latter is responsible for guiding its gene-silencing properties and actions. This is also why the protein is so important for RNAi. By learning to control how this molecule acts, researchers may soon be able to suppress or activate genes more efficiently.
Details of the new work appear in a study entitled “The structure of human Argonaute-2 in complex with miR-20a,” which is published in the May 24 issue of the esteemed medical journal Cell. The research was led by CSHL professor Leemor Joshua-Tor, PhD.
“Detailed knowledge of the structure of human Argonaute-2 and the way it interacts with its RNA guides will greatly improve our understanding of its biological mechanism of action,” says the scientist, who is also an investigator at the Howard Hughes Medical Institute.
“Such precise structural information of the human Argonaute bound to an important RNA guide could potentially aid both basic research to understand the function of genes and also advance the development of RNAi as a therapeutic strategy in clinical settings,” he goes on to say.
Funds for this research were secured from the Louis Morin Charitable Trust and a US National Institutes of Health (NIH) grant, the CSHL team says.
This investigation provides “the kind of information that might help us to design better synthetic guide RNAs for therapeutic use. It will also be useful to researchers who are trying to find more precise ways of blocking Argonaute activity,” Joshua-Tor adds.
He coauthored the new investigation with fellow HHMI investigator, Gregory Hannon, PhD.