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

Hölzl, H., Kapelari, B., Kellermann, J., Seemüller, E., Sümegi, M., Udvardy, A., et al. (2000). The regulatory complex of Drosophila melanogaster 26S proteasomes: Subunit composition and localization of a deubiquitylating enzyme. Journal of Cell Biology, 150(1), 119-129.

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Genre: Journal Article
Alternative Title : J. Cell Biol

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 Creators:
Hölzl, H.1, Author              
Kapelari, B.1, Author              
Kellermann, J.1, Author              
Seemüller, E.1, Author              
Sümegi, M., Author
Udvardy, A., Author
Medalia, O.1, Author              
Sperling, J., Author
Müller, S. A., Author
Engel, A., Author
Baumeister, W.1, Author              
Affiliations:
1External Organizations, ou_persistent22              

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Free keywords: Protein degradation; Ubiquitin; Ubiquitin hydrolase; Atp-dependent proteolysis; Electron microscopy.; Saccharomyces-cerevisiae proteasome; Rabbit reticulocyte lysate; C-terminal hydrolase; Electron-microscopy; 26-s proteasome; Deubiquitinating enzymes; Structural features; Ubiquitin system; Protein family; Atpase.; Cell & Developmental Biology in Current Contents(R)/Life Sciences.
 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. [References: 69]

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 Dates: 2000
 Publication Status: Published in print
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 Identifiers: eDoc: 318623
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Title: Journal of Cell Biology
  Alternative Title : J. Cell Biol
Source Genre: Journal
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Pages: - Volume / Issue: 150 (1) Sequence Number: - Start / End Page: 119 - 129 Identifier: -