Authors: | Parlati, F.; Weber, T.; McNew, J. A.; Westermann, B.; Söllner, T. H.; Rothman, J. E. |
Article Title: | Rapid and efficient fusion of phospholipid vesicles by the α-helical core of a SNARE complex in the absence of an N-terminal regulatory domain |
Abstract: | A protease-resistant core domain of the neuronal SNARE complex consists of an α-helical bundle similar to the proposed fusogenic core of vital fusion proteins [Skehel, J. J. and Wiley, D. C. (1998) Cell 95, 871-874]. We find that the isolated core of a SNARE complex efficiently fuses artificial bilayers and does so faster than full length SNAREs. Unexpectedly, a dramatic increase in speed results from removal of the N-terminal domain of the t- SNARE syntaxin, which does not affect the rate of assembly of v-t SNARES. In the absence of this negative regulatory domain, the half-time for fusion of an entire population of lipid vesicles by isolated SNARE cores (≃10 min) is compatible with the kinetics of fusion in many cell types. |
Keywords: | protein expression; nonhuman; protein domain; complex formation; protein degradation; nerve tissue proteins; membrane proteins; amino terminal sequence; kinetics; protein structure; protein determination; lipid bilayers; phospholipids; phospholipid; vesicular transport proteins; alpha helix; membrane fusion; syntaxin; qa-snare proteins; snare proteins; synaptosomal-associated protein 25; virus fusion protein; priority journal; article; phospholipid vesicle |
Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
Volume: | 96 |
Issue: | 22 |
ISSN: | 0027-8424 |
Publisher: | National Academy of Sciences |
Date Published: | 1999-10-26 |
Start Page: | 12565 |
End Page: | 12570 |
Language: | English |
DOI: | 10.1073/pnas.96.22.12565 |
PUBMED: | 10535962 |
PROVIDER: | scopus |
PMCID: | PMC22992 |
DOI/URL: | |
Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |