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TitlePro-CRISPR PcrIIC1-associated Cas9 system for enhanced bacterial immunity.
Journal, issue, pagesNature, Vol. 630, Issue 8016, Page 484-492, Year 2024
Publish dateMay 29, 2024
AuthorsShouyue Zhang / Ao Sun / Jing-Mei Qian / Shuo Lin / Wenjing Xing / Yun Yang / Han-Zhou Zhu / Xin-Yi Zhou / Yan-Shuo Guo / Yun Liu / Yu Meng / Shu-Lin Jin / Wenhao Song / Cheng-Ping Li / Zhaofu Li / Shuai Jin / Jian-Hua Wang / Meng-Qiu Dong / Caixia Gao / Chunlai Chen / Yang Bai / Jun-Jie Gogo Liu /
PubMed AbstractThe CRISPR system is an adaptive immune system found in prokaryotes that defends host cells against the invasion of foreign DNA. As part of the ongoing struggle between phages and the bacterial ...The CRISPR system is an adaptive immune system found in prokaryotes that defends host cells against the invasion of foreign DNA. As part of the ongoing struggle between phages and the bacterial immune system, the CRISPR system has evolved into various types, each with distinct functionalities. Type II Cas9 is the most extensively studied of these systems and has diverse subtypes. It remains uncertain whether members of this family can evolve additional mechanisms to counter viral invasions. Here we identify 2,062 complete Cas9 loci, predict the structures of their associated proteins and reveal three structural growth trajectories for type II-C Cas9. We found that novel associated genes (NAGs) tended to be present within the loci of larger II-C Cas9s. Further investigation revealed that CbCas9 from Chryseobacterium species contains a novel β-REC2 domain, and forms a heterotetrameric complex with an NAG-encoded CRISPR-Cas-system-promoting (pro-CRISPR) protein of II-C Cas9 (PcrIIC1). The CbCas9-PcrIIC1 complex exhibits enhanced DNA binding and cleavage activity, broader compatibility for protospacer adjacent motif sequences, increased tolerance for mismatches and improved anti-phage immunity, compared with stand-alone CbCas9. Overall, our work sheds light on the diversity and 'growth evolutionary' trajectories of II-C Cas9 proteins at the structural level, and identifies many NAGs-such as PcrIIC1, which serves as a pro-CRISPR factor to enhance CRISPR-mediated immunity.
External linksNature / PubMed:38811729
MethodsEM (single particle)
Resolution2.46 - 3.07 Å
Structure data

35827

8iyq

EMDB-35827, PDB-8iyq:
Structure of CbCas9 bound to 20-nucleotide complementary DNA substrate
Method: EM (single particle) / Resolution: 2.46 Å

37652

8wmh

EMDB-37652, PDB-8wmh:
Structure of CbCas9 bound to 6-nucleotide complementary DNA substrate
Method: EM (single particle) / Resolution: 2.6 Å

37656

8wmm

EMDB-37656, PDB-8wmm:
Structure of CbCas9-PcrIIC1 complex bound to 28-bp DNA substrate (20-nt complementary)
Method: EM (single particle) / Resolution: 2.98 Å

37657

8wmn

EMDB-37657, PDB-8wmn:
Structure of CbCas9-PcrIIC1 complex bound to 62-bp DNA substrate (symmetric 20-nt complementary)
Method: EM (single particle) / Resolution: 2.82 Å

37762

8wr4

EMDB-37762, PDB-8wr4:
Structure of CbCas9-PcrIIC1 complex bound to 62-bp DNA substrate (non-targeting complex)
Method: EM (single particle) / Resolution: 3.07 Å

Chemicals

ChemComp-MG:
Unknown entry

Source
  • chryseobacterium (bacteria)
KeywordsDNA BINDING PROTEIN/DNA/RNA / Cas9 complex / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA-RNA complex

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