Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps

Sonia K. Brady, Sarangapani Sreelatha, Yinnian Feng, Shishir P. S. Chundawat and Matthew J Lang ()
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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

Nature Communications, 2015, vol. 6, issue 1, 1-9

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms10149

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