SpringerProtocols: Abstract: Cell-Free Assay for Ubiquitin-Independent Proteasomal Protein Degradation

Cell-Free Assay for Ubiquitin-Independent Proteasomal Protein Degradation

By: Chaim Kahana³, Yuval Reiss⁴

Abstract

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The ATP-dependent degradation of ornithine decarboxylase is an exceptional case whereby a protein is targeted to the 26S proteasome independently of ubiquitin conjugation. Rather, prior association with the polyamine-induced regulatory protein, antizyme, confers susceptibility of ornithine decarboxylase to proteasomal degradation. In this chapter we describe ornithine decarboxylase/antizyme-based in vivo and in vitro systems for the measurement of ATP-dependent, ubiquitin-independent proteasomal degradation, as well as the application of ornithine decarboxylase as a reporter for the targeting of proteins to the 26S proteasome.

Affiliation(s): (3) Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot, Israel
(4) Proteologics Ltd., Rehovot Science Park, Rehovot, Israel

Book Title: Ubiquitin-Proteasome Protocols

Series: Methods in Molecular Biology | Volume: 301 | Pub. Date: Apr-01-2005 | Page Range: 83-96 | DOI: 10.1385/1-59259-895-1:083

Subject: Biochemistry

Key Words: 26S proteasome - ornithine decarboxylase - antizyme - antigen processing

References

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