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Seeing an explosive way of NSF/SNAP-mediated SNARE-complex disassembly using single-molecule measurements
류제경
 일시 
   2015년 4월 30일 (목) 오후 2시 (한국시간)
 연사 
   류제경 (KAIST)
세미나 개요
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 with a single burst reaction 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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관련논문 보기
Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover
Science, 27 March 2015: Vol. 347 no. 6229 pp. 1485-1489 | DOI: 10.1126/science.aaa5267
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