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. 2021 Mar 25;49(7):4120–4128. doi: 10.1093/nar/gkab179

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Dimerization, PAM recognition, and active site of Cas12f. (A) Dimerization interface of Cas12f mediated by REC1^C. (B) Substrate DNA cleavage assay using wild-type Cas12f and Cas12f with mutations in the dimerization interface. The results shown are representative of three experiments. (C) interaction between two REC2 domains of Cas12f.1 and Cas12f.2. (D) Interactions between the PAM duplex and Cas12f.1. Schematic of the interactions is shown on the right. (E) Substrate DNA cleavage assay using wild-type Cas12f and alanine substitutions for residues involved in PAM recognition. The results shown are representative of three experiments. (F) PAM binding site of Cas12f.2.