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Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

Author

Listed:
  • Sonia K. Brady

    (Vanderbilt University)

  • Sarangapani Sreelatha

    (SMART- BioSystems and Micromechanics, National University of Singapore)

  • Yinnian Feng

    (Vanderbilt University)

  • Shishir P. S. Chundawat

    (Rutgers, State University of New Jersey)

  • Matthew J Lang

    (Vanderbilt University
    SMART- BioSystems and Micromechanics, National University of Singapore
    Vanderbilt University)

Abstract

Cellobiohydrolase 1 from Trichoderma reesei (TrCel7A) processively hydrolyses cellulose into cellobiose. Although enzymatic techniques have been established as promising tools in biofuel production, a clear understanding of the motor’s mechanistic action has yet to be revealed. Here, we develop an optical tweezers-based single-molecule (SM) motility assay for precision tracking of TrCel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Our studies suggest TrCel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. Temperature-dependent kinetic studies establish the energy requirements for the fundamental stepping cycle, which likely includes energy from glycosidic bonds and other sources. Through SM measurements of isolated TrCel7A domains, we determine that the catalytic domain alone is sufficient for processive motion, providing insight into TrCel7A’s molecular motility mechanism.

Suggested Citation

  • Sonia K. Brady & Sarangapani Sreelatha & Yinnian Feng & Shishir P. S. Chundawat & Matthew J Lang, 2015. "Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps," Nature Communications, Nature, vol. 6(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms10149
    DOI: 10.1038/ncomms10149
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