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

Science (New York, N.Y.) 2015 Mar 27

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During intracellular membrane trafficking, N-ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment protein (α-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. Copyright © 2015, American Association for the Advancement of Science.

Citation

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. Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover. Science (New York, N.Y.). 2015 Mar 27;347(6229):1485-9