NDLI: Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel configurations.

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Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel configurations.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Weninger, Keith Chu, Steven Brunger, Axel T. Bowen, Mark E.
Description	Author Affiliation: Weninger K ( The Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305-4060, USA.);
Abstract	Vesicle fusion in eukaryotes is thought to involve the assembly of a highly conserved family of proteins termed soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) into a highly stable parallel four-helix bundle. We have used intermolecular single-molecule fluorescence resonance energy transfer to characterize preassembled neuronal SNARE complexes consisting of syntaxin, synaptobrevin, and synaptosome-associated protein of 25 kDa on deposited lipid bilayers. Surprisingly, we found a mixture of parallel as well as antiparallel configurations involving the SNARE motifs of syntaxin and synaptobrevin as well as those of syntaxin and synaptosome-associated protein of 25 kDa. The subpopulation with the parallel four-helix bundle configuration could be greatly enriched by an additional purification step in the presence of denaturant, indicating that the parallel configuration is the energetically most favorable state. Interconversion between the configurations was not observed. From this observation, we infer the conversion rate to be <1.5 h-1. The existence of antiparallel configurations suggests a regulatory role of chaperones, such as N-ethylmaleimide-sensitive factor, or the membrane environment during SNARE complex assembly in vivo, and it could be a partial explanation for the relatively slow rates of vesicle fusion observed by reconstituted fusion experiments in vitro.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	25
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Membrane Proteins Physiology Vesicular Transport Proteins Amino Acid Motifs Animals DNA, Complementary Metabolism Fluorescence Resonance Energy Transfer Gene Library Chemistry Models, Molecular Protein Binding Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Qa-SNARE Proteins R-SNARE Proteins SNARE Proteins Synaptosomes Time Factors Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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