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. 2021 Nov 25;12:6916. doi: 10.1038/s41467-021-27290-9

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a PAM-proximal residues involved in PAM recognition. Modeled structure of SpNG-LWQT (D1135L/S1136W/R1333Q/V1335T, residues shown in green) with 5′-CAT-3′ PAM based on SpNG (PDB ID: 6AI6). b Impact of mutating PAM-proximal residues on 5′-TGG-3′ (blue) and 5′-CAT-3′ (orange) PAM recognition. c PAM profile comparison between SpdNG-LWQT (gold) and SpdRY (green) against all NNN PAM libraries. d The influence of the fourth-position base on 5′-CAT-3′ PAM recognition of SpdNG-LWQT (gold) and SpdRY (green). e The repression effects of SpNG-LWQT (gold) and SpdRY (green) when targeting 5′-CAT-3′ PAM on both nontemplate and template strand. NTS nontemplate strand, TS template strand, RBS ribosome binding site. Data indicated the mean ± standard deviation (n = 3 independent biological replicates). Source data are provided as a Source Data file.