A Tale of Two Giant Proteases

Conference paper
Part of the Ernst Schering Foundation Symposium Proceedings book series (SCHERING FOUND, volume 2008/1)

Abstract

The 26S proteasome and tripeptidyl peptidase II (TPPII) are two exceptionally large eukaryotic protein complexes involved in intracellular proteolysis, where they exert their function sequentially: the proteasome, a multisubunit complex of 2.5 MDa, acts at the downstream end of the ubiquitin pathway and degrades ubiquitinylated proteins into small oligopeptides. Such oligopeptides are substrates for TPPII, a 6-MDa homooligomer, which releases tripeptides from their free N-terminus. Both 26S and TPPII are very fragile complexes refractory to crystallization and in their fully assembled native form have been visualized only by electron microscopy. Here, we will discuss the structural features of the two complexes and their functional implications.

Keywords

Intracellular Proteolysis Tripeptidyl Peptidase Ubiquitinylated Protein Proteolytic Core Proteolytic Chamber 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgements

We thank J. Peters for critically reading the manuscript.

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Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  1. 1.Department of Molecular Structural BiologyMax-Planck Institute of BiochemistryMartinsriedGermany

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