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Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function

Zaric, B. and Chami, M. and Remigy, H. and Engel, A. and Ballmer-Hofer, K. and Winkler, F. K. and Kambach, C.. (2005) Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function. Journal of biological chemistry, Vol. 280, H. 16. pp. 16066-16075.

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Official URL: http://edoc.unibas.ch/dok/A5262421

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Abstract

Sm and Sm-like (LSm) proteins form complexes engaging in various RNA-processing events. Composition and architecture of the complexes determine their intracellular distribution, RNA targets, and function. We have reconstituted the human LSm1-7 and LSm2-8 complexes from their constituent components in vitro. Based on the assembly pathway of the canonical Sm core domain, we used heterodimeric and heterotrimeric sub-complexes to assemble LSm1-7 and LSm2-8. Isolated sub-complexes form ring-like higher order structures. LSm1-7 is assembled and stable in the absence of RNA. LSm1-7 forms ring-like structures very similar to LSm2-8 at the EM level. Our in vitro reconstitution results illustrate likely features of the LSm complex assembly pathway. We prove the complexes to be functional both in an RNA bandshift and an in vivo cellular transport assay.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Engel, Andreas H and Chami, Mohamed
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 13:24

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