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Insights into the inhibition of type I-F CRISPR-Cas system by a multifunctional anti-CRISPR protein AcrIF24

Author

Listed:
  • Lingguang Yang

    (Beijing University of Chemical Technology
    Yichun University)

  • Laixing Zhang

    (Tsinghua University, Tsinghua-Peking Center for Life Sciences)

  • Peipei Yin

    (Beijing University of Chemical Technology
    Yichun University)

  • Hao Ding

    (Beijing University of Chemical Technology)

  • Yu Xiao

    (Tsinghua University, Tsinghua-Peking Center for Life Sciences)

  • Jianwei Zeng

    (Tsinghua University, Tsinghua-Peking Center for Life Sciences)

  • Wenhe Wang

    (Tsinghua University, Tsinghua-Peking Center for Life Sciences)

  • Huan Zhou

    (Chinese Academy of Sciences)

  • Qisheng Wang

    (Chinese Academy of Sciences)

  • Yi Zhang

    (Beijing University of Chemical Technology)

  • Zeliang Chen

    (Beijing University of Chemical Technology
    Shenyang Agricultural University)

  • Maojun Yang

    (Tsinghua University, Tsinghua-Peking Center for Life Sciences)

  • Yue Feng

    (Beijing University of Chemical Technology)

Abstract

CRISPR-Cas systems are prokaryotic adaptive immune systems and phages use anti-CRISPR proteins (Acrs) to counteract these systems. Here, we report the structures of AcrIF24 and its complex with the crRNA-guided surveillance (Csy) complex. The HTH motif of AcrIF24 can bind the Acr promoter region and repress its transcription, suggesting its role as an Aca gene in self-regulation. AcrIF24 forms a homodimer and further induces dimerization of the Csy complex. Apart from blocking the hybridization of target DNA to the crRNA, AcrIF24 also induces the binding of non-sequence-specific dsDNA to the Csy complex, similar to AcrIF9, although this binding seems to play a minor role in AcrIF24 inhibitory capacity. Further structural and biochemical studies of the Csy-AcrIF24-dsDNA complexes and of AcrIF24 mutants reveal that the HTH motif of AcrIF24 and the PAM recognition loop of the Csy complex are structural elements essential for this non-specific dsDNA binding. Moreover, AcrIF24 and AcrIF9 display distinct characteristics in inducing non-specific DNA binding. Together, our findings highlight a multifunctional Acr and suggest potential wide distribution of Acr-induced non-specific DNA binding.

Suggested Citation

  • Lingguang Yang & Laixing Zhang & Peipei Yin & Hao Ding & Yu Xiao & Jianwei Zeng & Wenhe Wang & Huan Zhou & Qisheng Wang & Yi Zhang & Zeliang Chen & Maojun Yang & Yue Feng, 2022. "Insights into the inhibition of type I-F CRISPR-Cas system by a multifunctional anti-CRISPR protein AcrIF24," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29581-1
    DOI: 10.1038/s41467-022-29581-1
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    References listed on IDEAS

    as
    1. M. Cemre Manav & Lan B. Van & Jinzhong Lin & Anders Fuglsang & Xu Peng & Ditlev E. Brodersen, 2020. "Structural basis for inhibition of an archaeal CRISPR–Cas type I-D large subunit by an anti-CRISPR protein," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    2. Alexander P. Hynes & Geneviève M. Rousseau & Daniel Agudelo & Adeline Goulet & Beatrice Amigues & Jeremy Loehr & Dennis A. Romero & Christophe Fremaux & Philippe Horvath & Yannick Doyon & Christian Ca, 2018. "Widespread anti-CRISPR proteins in virulent bacteriophages inhibit a range of Cas9 proteins," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    3. Rafael Pinilla-Redondo & Saadlee Shehreen & Nicole D. Marino & Robert D. Fagerlund & Chris M. Brown & Søren J. Sørensen & Peter C. Fineran & Joseph Bondy-Denomy, 2020. "Discovery of multiple anti-CRISPRs highlights anti-defense gene clustering in mobile genetic elements," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    4. Joe Bondy-Denomy & April Pawluk & Karen L. Maxwell & Alan R. Davidson, 2013. "Bacteriophage genes that inactivate the CRISPR/Cas bacterial immune system," Nature, Nature, vol. 493(7432), pages 429-432, January.
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