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New insight into an emerging genome-editing tool
Date:2/6/2014

high-resolution structures of the two major types of Cas9 proteins, we can start to see how this family of bacterial enzymes has evolved," Doudna says. "We see that the two structures are quite different from each other outside of their catalytic domains, suggesting an interesting structural plasticity that could explain how Cas9 is able to use different kinds of guide RNAs. Also, the differences in the two structures suggest that it may be possible to engineer smaller Cas9 variants and still retain function, an important goal for some genome engineering applications."

Doudna and Nogales are the corresponding authors, along with Martin Jinek of the University of Zurich, of a paper in Science that describes this research. The paper is titled "Structures of Cas9 endonucleases reveal RNA-mediated conformational activation." Co-authors are Fuguo Jiang, David Taylor, Samuel Sternberg, Emine Kaya, Enbo Ma, Carolin Anders, Michael Hauer, Kaihong Zhou, Steven Lin, Mattias Kaplan, Anthony Iavarone and Emmanuelle Charpentier.

Bacteria face a never-ending onslaught from viruses and invading strands of nucleic acid known as plasmids. To survive, they deploy a variety of defense mechanisms, including an adaptive-type nucleic acid-based immune system that revolves around a genetic element known as CRISPR, which stands for Clustered Regularly Interspaced Short Palindromic Repeats. Through the combination of CRISPR and squads of CRISPR-associated or "Cas" proteins, microbes are able to utilize small customized RNA molecules as guides to target and silence critical portions of an invader's genetic message and also to acquire immunity from similar invasions in the future.

Cas9 is a family of RNA-guided bacterial endonucleases employed by Type II CRISPR systems to recognize and cleave double-stranded DNA at site-specific sequences. Genetic engineers have begun harnessing Cas9 for genome editing and gene regulation in many eukaryotic organisms. Howev
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Contact: Lynn Yarris
lcyarris@lbl.gov
510-486-5375
DOE/Lawrence Berkeley National Laboratory
Source:Eurekalert  

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