Hexameric assembly of the proteasomal ATPases is templated through their C termini

Soyeon Park, Jeroen Roelofs, Woong Kim, Jessica Robert, Marion Schmidt, Steven P. Gygi and Daniel Finley ()
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Soyeon Park: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Jeroen Roelofs: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Woong Kim: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Jessica Robert: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Marion Schmidt: Albert Einstein College of Medicine, 1300 Morris Park Avenue, Forchheimer Building, Room 305, Bronx, New York 10461, USA
Steven P. Gygi: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA
Daniel Finley: Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA

Nature, 2009, vol. 459, issue 7248, 866-870

Abstract: Proteasome assembly The proteasome is a large proteolytic machine that degrades ubiquitin-tagged proteins. Substrates are recognized and unfolded by the regulatory particle (RP) and translocated into a central proteolytic chamber called the core particle (CP) where degradation takes place. The CP associates with the RP at either one or both ends. The RP can be further subdivided into the base and lid. Two studies from Finley and colleagues elucidate the pathway of RP assembly. They report the identification of three molecular chaperones that assist in the assembly of the RP. Assembly of the base proceeds through a complex consisting of five proteins, called BP1, which functions as an intermediate in the process. These studies show that RP assembly is a highly orchestrated process.

Date: 2009
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DOI: 10.1038/nature08065

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