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TitleInhibitory mechanism of CRISPR-Cas9 by AcrIIC4.
Journal, issue, pagesNucleic Acids Res, Vol. 51, Issue 17, Page 9442-9451, Year 2023
Publish dateSep 22, 2023
AuthorsXuzichao Li / Fumeng Liao / Jiaqi Gao / Guangyong Song / Chendi Zhang / Nan Ji / Xiaoshen Wang / Jing Wen / Jia He / Yong Wei / Heng Zhang / Zhuang Li / Guimei Yu / Hang Yin /
PubMed AbstractCRISPR-Cas systems act as the adaptive immune systems of bacteria and archaea, targeting and destroying invading foreign mobile genetic elements (MGEs) such as phages. MGEs have also evolved anti- ...CRISPR-Cas systems act as the adaptive immune systems of bacteria and archaea, targeting and destroying invading foreign mobile genetic elements (MGEs) such as phages. MGEs have also evolved anti-CRISPR (Acr) proteins to inactivate the CRISPR-Cas systems. Recently, AcrIIC4, identified from Haemophilus parainfluenzae phage, has been reported to inhibit the endonuclease activity of Cas9 from Neisseria meningitidis (NmeCas9), but the inhibition mechanism is not clear. Here, we biochemically and structurally investigated the anti-CRISPR activity of AcrIIC4. AcrIIC4 folds into a helix bundle composed of three helices, which associates with the REC lobe of NmeCas9 and sgRNA. The REC2 domain of NmeCas9 is locked by AcrIIC4, perturbing the conformational dynamics required for the target DNA binding and cleavage. Furthermore, mutation of the key residues in the AcrIIC4-NmeCas9 and AcrIIC4-sgRNA interfaces largely abolishes the inhibitory effects of AcrIIC4. Our study offers new insights into the mechanism of AcrIIC4-mediated suppression of NmeCas9 and provides guidelines for the design of regulatory tools for Cas9-based gene editing applications.
External linksNucleic Acids Res / PubMed:37587688 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.8 - 3.52 Å
Structure data

36123

8ja0

EMDB-36123, PDB-8ja0:
Cryo-EM structure of the NmeCas9-sgRNA-AcrIIC4 ternary complex
Method: EM (single particle) / Resolution: 3.52 Å

PDB-7xvq:
Crystal structure of AcrIIC4
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • neisseria meningitidis (bacteria)
  • haemophilus parainfluenzae (bacteria)
KeywordsANTIMICROBIAL PROTEIN / RNA BINDING PROTEIN/RNA / a protein complex / VIRAL PROTEIN / RNA BINDING PROTEIN-RNA complex

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