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Related Experiment Videos

Folding intermediates of SNARE complex assembly.

K M Fiebig1, L M Rice, E Pollock

  • 1The Howard Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.

Nature Structural Biology
|February 27, 1999
PubMed
Summary

This study used NMR spectroscopy to reveal how yeast SNARE proteins assemble. The findings suggest a sequential assembly process that drives membrane fusion.

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Area of Science:

  • Structural Biology
  • Molecular Biophysics
  • Cell Biology

Background:

  • Soluble NSF attachment protein receptor (SNARE) proteins are crucial for vesicle-membrane fusion.
  • Understanding SNARE complex assembly is key to elucidating the mechanism of membrane fusion.
  • Previous studies have indicated the importance of SNARE protein interactions in cellular processes.

Purpose of the Study:

  • To characterize the structural dynamics of yeast SNARE complex assembly.
  • To investigate the conformational changes of Sso1 upon binding with Sec9 and Snc1.
  • To elucidate the sequential steps involved in SNARE complex formation and its role in membrane fusion.

Main Methods:

  • Solution nuclear magnetic resonance (NMR) spectroscopy was employed to analyze SNARE complex structures.

Related Experiment Videos

  • Three distinct assembly states were characterized: Sso1 alone, Sso1-Sec9 binary complex, and Sso1-Sec9-Snc1 ternary complex.
  • Analysis focused on conformational changes and the induction of secondary structure during complex formation.

    • Main Results:

    • Sso1 exists in a 'closed' conformation, likely a four-helix bundle with flexible flanking regions.
    • Binding of Sec9 induces an 'open' state in Sso1, suggesting conformational switching as a regulatory mechanism.
    • Formation of binary and ternary complexes promotes alpha-helical structure in previously unstructured regions of Sec9 and Snc1.

    Conclusions:

    • SNARE complex assembly appears to be a directed, sequential process starting from regions distal to the membrane.
    • This assembly mechanism facilitates the bringing of membranes into close proximity, potentially leading to fusion.
    • Conformational flexibility and switching in SNARE proteins play a critical role in regulating membrane fusion.