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  A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy

Rockel, B., Peters, J., Kühlmorgen, B., Glaeser, R. M., & Baumeister, W. (2002). A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy. EMBO Journal, 21(22), 5979-5984.

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Genre: Journal Article
Alternative Title : Embo J.

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 Creators:
Rockel, B.1, Author              
Peters, J.1, Author              
Kühlmorgen, B., Author
Glaeser, R. M., Author
Baumeister, W.2, Author              
Affiliations:
1External Organizations, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: cryo-electron microscopy; three-dimensional reconstruction; tripeptidyl peptidase II
 Abstract: Tripeptidyl peptidase II (TPP II) is an exopeptidase of the subtilisin type of serine proteases that is thought to act downstream of the proteasome in the ubiquitin-proteasome pathway. Recently, a key role in a pathway parallel to the ubiquitin-proteasome pathway has been ascribed to TPP 11, which forms a giant protease complex in mammalian cells. Here, we report the 900-fold purification of TPP II from Drosophila eggs and demonstrate via cryo-electron microscopy that TPP II from Drosophila melanogaster also forms a giant protease complex. The presented three-dimensional reconstruction of the 57 X 27 nm TPP II complex at 3.3 nm resolution reveals that the 150 kDa subunits form a superstructure composed of two segmented and twisted strands. Each strand is 12.5 nm in width and composed of 11 segments that enclose a central channel.

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Language(s): eng - English
 Dates: 2002-11-15
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41668
ISI: 000179446900004
 Degree: -

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Title: EMBO Journal
  Alternative Title : Embo J.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 21 (22) Sequence Number: - Start / End Page: 5979 - 5984 Identifier: ISSN: 0261-4189