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Assembly and substrate recognition of curli biogenesis system

Author

Listed:
  • Zhaofeng Yan

    (Key Laboratory of Protein Sciences (Tsinghua University), Ministry of Education
    Tsinghua University
    Tsinghua University)

  • Meng Yin

    (Key Laboratory of Protein Sciences (Tsinghua University), Ministry of Education
    Tsinghua University
    Tsinghua University
    Tsinghua-Peking Joint Center for Life Sciences)

  • Jianan Chen

    (Key Laboratory of Protein Sciences (Tsinghua University), Ministry of Education
    Tsinghua University
    Tsinghua University)

  • Xueming Li

    (Key Laboratory of Protein Sciences (Tsinghua University), Ministry of Education
    Tsinghua University
    Tsinghua University
    Tsinghua-Peking Joint Center for Life Sciences)

Abstract

A major component of bacterial biofilms is curli amyloid fibrils secreted by the curli biogenesis system. Understanding the curli biogenesis mechanism is critical for developing therapeutic agents for biofilm-related infections. Here we report a systematic study of the curli biogenesis system, highlighted by structural, biochemical and functional analysis of the secretion channel complexes (CsgF-CsgG) with and without the curli substrate. The dual-pore architecture of the CsgF-CsgG complex was observed and used to develop an approach to inhibit the curli secretion by physically reducing the size of the CsgF pore. We further elucidated the assembly of the CsgFG complex with curli components (CsgA and CsgB) and curli-cell association through CsgF. Importantly, the recognition of the CsgA substrate by CsgG was uncovered. Nine crevices outside of the CsgG channel provide specific and highly-conserved recognition sites for CsgA N-terminus. Together with analysis of CsgE, our study provides comprehensive insights into curli biogenesis.

Suggested Citation

  • Zhaofeng Yan & Meng Yin & Jianan Chen & Xueming Li, 2020. "Assembly and substrate recognition of curli biogenesis system," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-019-14145-7
    DOI: 10.1038/s41467-019-14145-7
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    Cited by:

    1. Mike Sleutel & Brajabandhu Pradhan & Alexander N. Volkov & Han Remaut, 2023. "Structural analysis and architectural principles of the bacterial amyloid curli," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Hema M. Swasthi & Joseph L. Basalla & Claire E. Dudley & Anthony G. Vecchiarelli & Matthew R. Chapman, 2023. "Cell surface-localized CsgF condensate is a gatekeeper in bacterial curli subunit secretion," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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