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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: Zeitschriftenartikel
Alternativer Titel : J. Cell Biol

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

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Schlagwörter: 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.
 Zusammenfassung: 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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 Datum: 2000
 Publikationsstatus: Erschienen
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 Identifikatoren: eDoc: 318623
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Titel: Journal of Cell Biology
  Alternativer Titel : J. Cell Biol
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 150 (1) Artikelnummer: - Start- / Endseite: 119 - 129 Identifikator: -