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The regulatory complex of Drosophila melanogaster 26S proteasomes : subunit composition and localization of a deubiquitylating enzyme

Holzl, H. and Kapelari, B. and Kellermann, J. and Seemuller, E. and Sumegi, M. and Udvardy, A. and Medalia, O. and Sperling, J. and Müller, S. A. and Engel, A. and Baumeister, W.. (2000) The regulatory complex of Drosophila melanogaster 26S proteasomes : subunit composition and localization of a deubiquitylating enzyme. The Journal of cell biology, Vol. 150, H. 1. pp. 119-130.

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Official URL: http://edoc.unibas.ch/dok/A5262370

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Abstract

Drosophila melanogaster embryos are a source for homogeneous and stable 26S proteasomes suitable for structural studies. For biochemical characterization, purified 26S proteasomes were resolved by two- dimensional (2D) gel electrophoresis and subunits composing the regulatory complex (RC) were identified by amino acid sequencing and immunoblotting, before corresponding cDNAs were sequenced. 17 subunits from Drosophila RCs were found to have homologues in the yeast and human RCs. An additional subunit, p37A, not yet described in RCs of other organisms, is a member of the ubiquitin COOH-terminal hydrolase family (UCH). Analysis of EM images of 26S proteasomes-UCH-inhibitor complexes allowed for the first time to localize one of the RC's specific functions, deubiquitylating activity.The masses of 26S proteasomes with either one or two attached RCs were determined by scanning transmission EM (STEM), yielding a mass of 894 kD for a single RC. This value is in good agreement with the summed masses of the 18 identified RC subunits (932 kD), indicating that the number of subunits is complete.
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:Rockefeller University Press
ISSN:0021-9525
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:31 Dec 2015 10:43
Deposited On:22 Mar 2012 13:23

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