Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover
| Autor: | Yongsoo Park, Tae-Young Yoon, Ho Min Kim, Reinhard Jahn, Soo Jin Kim, Duyoung Min, Je-Kyung Ryu, Changbong Hyeon, Sang Hyun Rah, Haesoo Kim |
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| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Multidisciplinary
Chemistry Hydrolysis Lipid bilayer fusion Random hexamer Exocytosis Article Rats Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins chemistry.chemical_compound Adenosine Triphosphate Spectrometry Fluorescence Biochemistry ATP hydrolysis Cricetinae Biophysics Fluorescence Resonance Energy Transfer Animals Cattle Soluble NSF attachment protein SNARE complex SNARE Proteins Adenosine triphosphate N-Ethylmaleimide-Sensitive Proteins |
| Zdroj: | Science |
| Popis: | An explosive way to fuse membranes The molecular machine that promotes membrane fusion during intracellular transport involves a number of so-called SNARE proteins. Ryu et al. describe the molecular mechanism by which two proteins —NSF and α-SNAP—disassemble SNARE complexes. A combination of single-molecule techniques resolved intermediate steps of the reaction. Surprisingly, unlike previously assumed, NSF did not unwind SNARE complexes processively. Instead, built-up tension was released in a single burst to “tear” the SNARE complex apart in a one-step global unfolding reaction. Science , this issue p. 1485 |
| Databáze: | OpenAIRE |
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