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  A revised model for the oligomeric state of the n-ethylmaleimide-sensitive fusion protein, nsf

Fleming, K. G., Hohl, T. M., Yu, R. C., Müller, S. A., Wolpensinger, B., Engel, A., et al. (1998). A revised model for the oligomeric state of the n-ethylmaleimide-sensitive fusion protein, nsf. Journal of Biological Chemistry, 273(25), 15675-15681.

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Fleming, K. G., Author
Hohl, T. M., Author
Yu, R. C., Author
Müller, S. A., Author
Wolpensinger, B., Author
Engel, A., Author
Engelhardt, H.1, Author              
Brünger, A. T., Author
Söllner, T. H., Author
Hanson, P. I., Author
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1External Organizations, ou_persistent22              

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Free keywords: Vesicular transport; Electron-microscopy; Boundary analysis; Light-scattering; Membrane-fusion; Alpha-snap; Complex; Atp; Docking; Macromolecules.; Biochemistry & biophysics.
 Abstract: The N-ethylmaleimide-sensitive fusion protein (NSF) is an ATPase that plays an essential role in intracellular membrane trafficking, Previous reports have concluded that NSF forms either a tetramer or a trimer in solution, and that assembly of the oligomer is essential for efficient activity in membrane transport reactions. However, in recent electron microscopic analyses NSF appears as a hexagonal cylinder similar in size to related ATPases known to be hexamers. We have therefore reevaluated NSF's oligomeric state using a variety of quantitative biophysical techniques. Sedimentation equilibrium and sedimentation velocity analytical ultracentrifugation, transmission electron microscopy with rotational image analysis, scanning transmission electron microscopy, and multiangle light scattering all demonstrate that, in the presence of nucleotide, NSF is predominantly a hexamer. Sedimentation equilibrium results further suggest that the NSF hexamer is held together by oligomerization of its D2 domains. The sedimentation coefficient, s(20,w)(0), of 13.4 (+/-0.1) S indicates that NSF has unusual hydrodynamic characteristics that cannot be solely explained by its shape. The demonstration that NSF is a hexameric oligomer highlights structural similarities between it and several related ATPases which act by switching the conformational states of their protein substrates in order to activate them for subsequent reactions. [References: 39]

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 Dates: 1998-06-19
 Publication Status: Published in print
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 Identifiers: eDoc: 318703
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 273 (25) Sequence Number: - Start / End Page: 15675 - 15681 Identifier: -