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Publication Abstract from PubMed

The Type VI-D CRISPR-Cas system employs an RNA-guided RNase Cas13d with minimal targeting constraints to combat viral infections. This CRISPR system contains RspWYL1 as a unique accessory protein that plays a key role in boosting its effector function on target RNAs, but the mechanism behind this RspWYL1-mediated stimulation remains completely unexplored. Through structural and biophysical approaches, we reveal that the full-length RspWYL1 possesses a novel three-domain architecture and preferentially binds ssRNA with high affinity. Specifically, the N-terminus of RspWYL1 harbors a ribbon-helix-helix motif reminiscent of transcriptional regulators; the central WYL domain of RspWYL1 displays a Sm-like beta-barrel fold; and the C-terminal domain of RspWYL1 primarily contributes to the dimerization of RspWYL1 and may regulate the RspWYL1 function via a large conformational change. Collectively, this study provides a first glimpse into the complex mechanism behind the RspWYL1-dictated boosting of target ssRNA cleavage in the Type VI-D CRISPR-Cas system.

Structural insights into the modulatory role of the accessory protein WYL1 in the Type VI-D CRISPR-Cas system.,Zhang H, Dong C, Li L, Wasney GA, Min J Nucleic Acids Res. 2019 Apr 12. pii: 5446253. doi: 10.1093/nar/gkz269. PMID:30976796^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.