The proteasome - a macromolecular assembly designed to confine proteolysis to a 
nanocompartment

Baumeister, W.; Cejka, Z.; Kania, M.; Seemüller, E.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

The proteasome - a macromolecular assembly designed to confine proteolysis to a nanocompartment

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Baumeister, W., Cejka, Z., Kania, M., & Seemüller, E. (1997). The proteasome - a macromolecular assembly designed to confine proteolysis to a nanocompartment. Biological Chemistry, 378(3-4), 121-130.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-72B6-2

Abstract

Significant progress has been made over the past few years in elucidating the structural principles and the enzymatic mechanism of the 20S proteasome. As a result, the proteasome has become the prototype of a new family of enzymes, the Ntn hydrolases, as well as a paradigm for macromolecular assemblies that confine their proteolytic activity to an inner nanocompartment. Since access to this nanocompartment is restricted to unfolded substrate polypeptides, the 20S proteasome must be functionally linked to a substrate recognition and unfolding machinery. In eukaryotes this is provided by the 19S 'cap' complex, which associates with the 20S core to form the 26S proteasome, a protease capable of degrading ubiquitinated proteins in an ATP-dependent manner. [References: 88]