Mechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanism

Duyoung Min, Kipom Kim, Changbong Hyeon, Yong Hoon Cho, Yeon-Kyun Shin () and Tae-Young Yoon ()
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Duyoung Min: National Creative Research Initiative Center for Single-Molecule Systems Biology, KAIST
Kipom Kim: KAIST
Changbong Hyeon: School of Computational Sciences, Korea Institute for Advanced Study
Yong Hoon Cho: KAIST
Yeon-Kyun Shin: Biomedical Research Institute, Korea Institute of Science and Technology
Tae-Young Yoon: National Creative Research Initiative Center for Single-Molecule Systems Biology, KAIST

Nature Communications, 2013, vol. 4, issue 1, 1-10

Abstract: Abstract Formation of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex provides mechanical thrust for membrane fusion, but its molecular mechanism is still unclear. Here using magnetic tweezers, we observe mechanical responses of a single neuronal SNARE complex under constant pulling force. Single SNARE complexes may be unzipped with 34 pN force. When rezipping is induced by lowering the force to 11 pN, only a partially assembled state results, with the C-terminal half of the SNARE complex remaining disassembled. Reassembly of the C-terminal half occurs only when the force is further lowered below 11 pN. Thus, mechanical hysteresis, characterized by the unzipping and rezipping cycle of a single SNARE complex, produces the partially assembled state. In this metastable state, unzipping toward the N-terminus is suppressed while zippering toward the C-terminus is initiated as a steep function of force. This ensures the directionality of SNARE-complex formation, making the SNARE complex a robust force-generating machine.

Date: 2013
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DOI: 10.1038/ncomms2692

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