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Molecular mass, stoichiometry, and assembly of 20 s particles

Wimmer, C. and Hohl, T. M. and Hughes, C. A. and Müller, S. A. and Sollner, T. H. and Engel, A. and Rothman, J. E.. (2001) Molecular mass, stoichiometry, and assembly of 20 s particles. Journal of biological chemistry, Vol. 276 , no. 31. pp. 29091-29097.

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Official URL: http://edoc.unibas.ch/dok/A5262386

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Abstract

N-Ethylmaleimide-sensitive factor (NSF), soluble NSF attachment proteins (SNAPs), and SNAP receptor (neuronal SNARE) complexes form 20 S particles with a mass of 788 +/- 122 kDa as judged by scanning transmission electron microscopy. A single NSF hexamer and three alphaSNAP monomers reside within a 20 S particle as determined by quantitative amino acid analysis. In order to study the binding of alphaSNAP and NSF in solution, to define their binding domains, and to specify the role of oligomerization in their interaction, we fused domains of alphaSNAP and NSF to oligomerization modules derived from thrombospondin-1, a trimer, and cartilage oligomeric matrix protein, a pentamer, respectively. Binding studies with these fusion proteins reproduced the interaction of alphaSNAP and NSF N domains in the absence of the hexamerization domain of NSF (D2). Trimeric alphaSNAP (or its C-terminal half) is sufficient to recruit NSF even in the absence of SNARE complexes. Furthermore, pentameric NSF N domains are able to bind alphaSNAP in complex with SNAREs, whereas monomeric N domains do not. Our results demonstrate that the oligomerization of both NSF N domains and alphaSNAP provides a critical driving force for their interaction and the assembly of 20 S particles.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Engel, Andreas H and Müller, Shirley
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:American Society of Biological Chemists
ISSN:0021-9258
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:21
Deposited On:22 Mar 2012 13:23

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