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Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases

Author

Listed:
  • M. A. Jackson

    (The University of Queensland)

  • E. K. Gilding

    (The University of Queensland)

  • T. Shafee

    (La Trobe University)

  • K. S. Harris

    (La Trobe University)

  • Q. Kaas

    (The University of Queensland)

  • S. Poon

    (La Trobe University)

  • K. Yap

    (The University of Queensland)

  • H. Jia

    (The University of Queensland)

  • R. Guarino

    (La Trobe University)

  • L. Y. Chan

    (The University of Queensland)

  • T. Durek

    (The University of Queensland)

  • M. A. Anderson

    (La Trobe University)

  • D. J. Craik

    (The University of Queensland)

Abstract

Asparaginyl endopeptidases (AEPs) are proteases that have crucial roles in plant defense and seed storage protein maturation. Select plant AEPs, however, do not function as proteases but as transpeptidases (ligases) catalyzing the intra-molecular ligation of peptide termini, which leads to peptide cyclization. These ligase-type AEPs have potential biotechnological applications ranging from in vitro peptide engineering to plant molecular farming, but the structural features enabling these enzymes to catalyze peptide ligation/cyclization rather than proteolysis are currently unknown. Here, we compare the sequences, structures, and functions of diverse plant AEPs by combining molecular modeling, sequence space analysis, and functional testing in planta. We find that changes within the substrate-binding pocket and an adjacent loop, here named the “marker of ligase activity”, together play a key role for AEP ligase efficiency. Identification of these structural determinants may facilitate the discovery of more ligase-type AEPs and the engineering of AEPs with tailored catalytic properties.

Suggested Citation

  • M. A. Jackson & E. K. Gilding & T. Shafee & K. S. Harris & Q. Kaas & S. Poon & K. Yap & H. Jia & R. Guarino & L. Y. Chan & T. Durek & M. A. Anderson & D. J. Craik, 2018. "Molecular basis for the production of cyclic peptides by plant asparaginyl endopeptidases," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04669-9
    DOI: 10.1038/s41467-018-04669-9
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    Cited by:

    1. Yue Zeng & Wei Shi & Zhi Liu & Hao Xu & Liya Liu & Jiaying Hang & Yongqin Wang & Mengru Lu & Wei Zhou & Wei Huang & Feng Tang, 2023. "C-terminal modification and functionalization of proteins via a self-cleavage tag triggered by a small molecule," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Edward K. Gilding & Mark A. Jackson & Linh T. T. Nguyen & Brett R. Hamilton & Katherine A. Farquharson & Wing L. Ho & Kuok Yap & Carolyn J. Hogg & Katherine Belov & David J. Craik, 2024. "Hijacking of N-fixing legume albumin-1 genes enables the cyclization and stabilization of defense peptides," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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