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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-BCA7-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CCD3-E
Genre: Journal Article

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 Creators:
Ryu, J. K., Author
Min, D., Author
Rah, S. H., Author
Kim, S. J., Author
Park, Y.1, Author              
Kim, H., Author
Hyeon, C., Author
Kim, H. M., Author
Jahn, R.1, Author              
Yoon, T. Y., Author
Affiliations:
1Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society, ou_578595              

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 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.

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Language(s): eng - English
 Dates: 2015-03-27
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1126/science.aaa5267
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 347 (6229) Sequence Number: - Start / End Page: 1485 - 1489 Identifier: -