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Molecular and Cellular Biology, July 2000, p. 4691-4698, Vol. 20, No. 13
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Evidence for an Interaction between Ubiquitin-Conjugating Enzymes and the 26S Proteasome

Prasad Tongaonkar,dagger Li Chen, David Lambertson, Bom Ko, and Kiran Madura*

Department of Biochemistry, Robert Wood Johnson Medical School---UMDNJ, Piscataway, New Jersey 08854

Received 9 February 2000/Returned for modification 3 March 2000/Accepted 31 March 2000

The targeting of proteolytic substrates is accomplished by a family of ubiquitin-conjugating (E2) enzymes and a diverse set of substrate recognition (E3) factors. The ligation of a multiubiquitin chain to a substrate can promote its degradation by the proteasome. However, the mechanism that facilitates the translocation of a substrate to the proteasome in vivo is poorly understood. We have discovered that E2 proteins, including Ubc1, Ubc2, Ubc4, and Ubc5, can interact with the 26S proteasome. Significantly, the interaction between Ubc4 and the proteasome is strongly induced by heat stress, consistent with the requirement for this E2 for efficient stress tolerance. A catalytically inactive derivative of Ubc4 (Ubc4C86A), which causes toxicity in yeast cells, can also bind the proteasome. Purified proteasomes can ligate ubiquitin to a test substrate without the addition of exogenous E2 protein, suggesting that the ubiquitylation of some proteolytic substrates might be directly coupled to degradation by the proteasome.

* Corresponding author. Mailing address: Department of Biochemistry, Room 628, Robert Wood Johnson Medical School---UMDNJ, 675 Hoes Ln., Piscataway, NJ 08854. Phone: (732) 235-5602. Fax: (732) 235-4783. E-mail: maduraki{at}umdnj.edu.

dagger Present address: Department of Biological Chemistry, University of California, Irvine, CA 92697.

Molecular and Cellular Biology, July 2000, p. 4691-4698, Vol. 20, No. 13
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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