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Journal Article

Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover.

MPS-Authors
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Park,  Y.
Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Ryu, J. K., Min, D., Rah, S. H., Kim, S. J., Park, Y., Kim, H., et al. (2015). Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover. Science, 347(6229), 1485-1489. doi:10.1126/science.aaa5267.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0026-BCA7-A
Abstract
During intracellular membrane trafficking, N-ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment protein (alpha-SNAP) disassemble the soluble NSF attachment protein receptor (SNARE) complex for recycling of the SNARE proteins. The molecular mechanism by which NSF disassembles the SNARE complex is largely unknown. Using single-molecule fluorescence spectroscopy and magnetic tweezers, we found that NSF disassembled a single SNARE complex in only one round of adenosine triphosphate (ATP) turnover. Upon ATP cleavage, the NSF hexamer developed internal tension with dissociation of phosphate ions. After latent time measuring tens of seconds, NSF released the built-up tension in a burst within 20 milliseconds, resulting in disassembly followed by immediate release of the SNARE proteins. Thus, NSF appears to use a "spring-loaded" mechanism to couple ATP hydrolysis and unfolding of substrate proteins.