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

Je Kyung Ryu, Duyoung Min, Sang Hyun Rah, Soo Jin Kim, Yongsoo Park, Haesoo Kim, Changbong Hyeon, Ho Min Kim, Reinhard Jahn*, Tae Young Yoon

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

74 Citations (Scopus)

Abstract

During intracellular membrane trafficking, N-ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment protein (a-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.

Original languageEnglish
Pages (from-to)1485-1489
Number of pages5
JournalScience
Volume347
Issue number6229
DOIs
Publication statusPublished - 27 Mar 2015
Externally publishedYes

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