High-resolution structure of cas13b and biochemical characterization of RNA targeting and cleavage

(Cell Reports 26, 3741–3751.e1–e5; March 26, 2019) In our paper, we reported the structure and biochemical characterization of the RNA-guided RNase Cas13b from Prevotella buccae (PbuCas13b). This work included an assessment of the turnover rate of this enzyme. Recently, it was brought to our attention by Juan Santiago and Ashwin Ramachandran that the reported turnover rate was inconsistent with our data (Figure 5D). Upon re-evaluation of our raw data, we found an error in the units. The corrected plot now appears online and is shown below, and the corrected turnover rate is 0.955 s-1. The error does not affect the conclusions of the paper with regard to either the structure or mechanism of action. We apologize for any confusion this error may have caused. High-Resolution Structure of Cas13b and Biochemical Characterization of RNA Targeting and CleavageSlaymaker et al.Cell ReportsMarch 26, 2019In BriefSlaymaker et al. present a high-resolution structure of Cas13b in combination with biochemical studies showing that Cas13b is a highly dynamic, multi-turnover enzyme distinct from other Cas13 family members. Additionally, the authors demonstrate Cas13b can be rationally engineered to change RNA cleavage specificity and create a minimal variant suitable for delivery with viral vectors. Full-Text PDF Open Access