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  Structural features of the 26 S proteasome complex

Peters, J. M., Cejka, Z., Harris, J. R., Kleinschmidt, J. A., & Baumeister, W. (1993). Structural features of the 26 S proteasome complex. Journal of Molecular Biology., 234(4), 932-937.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-73CD-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-73CE-6
Genre: Journal Article

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Peters, J. M., Author
Cejka, Z., Author
Harris, J. R., Author
Kleinschmidt, J. A., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Animal; *Cysteine Endopeptidases/ch [Chemistry]; Electrophoresis, Gel, Two-Dimensional; Image Processing, Computer-Assisted; Microscopy, Electron; *Multienzyme Complexes/ch [Chemistry]; Oocytes/en [Enzymology]; Xenopus laevis
 Abstract: Proteasomes play a key role in the degradation of abnormal proteins, of short-lived regulatory proteins and in antigen processing. Evidence is accumulating that the 20 S proteasome represents the proteolytic core of the 26 S protease complex (26 S proteasome) which contains several additional subunits implicated in regulation and substrate recognition. Using electron microscopy and digital image analysis we obtained first insights into the structure of this complex which has an estimated molecular weight of approximately 2000 kDa. Two highly asymmetric masses which presumably contain the regulatory subunits of the 26 S complex are attached to both ends of the dimeric 20 S proteasome clearly reflecting its C2 symmetry. The structural uniformity of the complex, i.e. the absence of significant inter-image variations, has important implications for the structure of the latter: It indicates that, in spite of their sequence similarities, the various alpha-type and beta-type subunits of the 20 S proteasome are not promiscuous but occupy precisely defined positions.

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 Dates: 1993
 Publication Status: Published in print
 Pages: -
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 Rev. Method: -
 Identifiers: eDoc: 318699
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Title: Journal of Molecular Biology.
Source Genre: Journal
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Pages: - Volume / Issue: 234 (4) Sequence Number: - Start / End Page: 932 - 937 Identifier: -