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  Extreme parsimony in ATP consumption by 20S complexes in the global disassembly of single SNARE complexes

Kim, C., Shon, M. J., Kim, S. H., Eun, G. S., Ryu, J.-K., Hyeon, C., et al. (2021). Extreme parsimony in ATP consumption by 20S complexes in the global disassembly of single SNARE complexes. Nature Communications, 12: 3206. doi:10.1038/s41467-021-23530-0.

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 Creators:
Kim, C., Author
Shon, M. J., Author
Kim, S. H., Author
Eun, G. S., Author
Ryu, J.-K., Author
Hyeon, C., Author
Jahn, R.1, Author              
Yoon, T.-Y., Author
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1Laboratory of Neurobiology, Max Planck Institute for Biophysical Chemistry, Max Planck Society, ou_3049887              

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Free keywords: Enzyme mechanisms; Single-molecule biophysics
 Abstract: Fueled by ATP hydrolysis in N-ethylmaleimide sensitive factor (NSF), the 20S complex disassembles rigid SNARE (soluble NSF attachment protein receptor) complexes in single unraveling step. This global disassembly distinguishes NSF from other molecular motors that make incremental and processive motions, but the molecular underpinnings of its remarkable energy efficiency remain largely unknown. Using multiple single-molecule methods, we found remarkable cooperativity in mechanical connection between NSF and the SNARE complex, which prevents dysfunctional 20S complexes that consume ATP without productive disassembly. We also constructed ATP hydrolysis cycle of the 20S complex, in which NSF largely shows randomness in ATP binding but switches to perfect ATP hydrolysis synchronization to induce global SNARE disassembly, minimizing ATP hydrolysis by non-20S complex-forming NSF molecules. These two mechanisms work in concert to concentrate ATP consumption into functional 20S complexes, suggesting evolutionary adaptations by the 20S complex to the energetically expensive mechanical task of SNARE complex disassembly.

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Language(s): eng - English
 Dates: 2021-05-28
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-021-23530-0
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Title: Nature Communications
Source Genre: Journal
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Pages: 15 Volume / Issue: 12 Sequence Number: 3206 Start / End Page: - Identifier: -