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Papers In Press, published online ahead of print May 21, 2001
J. Biol. Chem, 10.1074/jbc.M103378200
Submitted on April 16, 2001
Revised on May 21, 2001
Accepted on May 18, 2001

In vitro assembly and recognition of K63 polyubiquitin chains

Roseanne M. Hofmann and Cecile M. Pickart

Department of Biochemistry and Molecular Biology, The Johns Hopkins University, Baltimore, MD 21205

Corresponding Author: cpickart{at}welchlink.welch.jhu.edu

Polyubiquitin chains assembled through lysine-48 (K48) of ubiquitin act as a signal for substrate proteolysis by 26S proteasomes, whereas chains assembled through K63 play a mechanistically undefined role in postreplicative DNA repair. We showed previously that the products of the UBC13 and MMS2 genes function in error-free postreplicative DNA repair in the yeast Saccharomyces cerevisiae and form a complex that assembles K63-linked polyubiquitin chains in vitro. Here we confirm that the Mms2/Ubc13 complex functions as a high-affinity heterodimer in the chain assembly reaction in vitro, and report the results of a kinetic characterization of the polyubiquitin chain assembly reaction. To test whether a K63-linked polyubiquitin chain can signal degradation, we conjugated K63-linked tetraubiquitin to a model substrate of 26S proteasomes. Although the noncanonical chain effectively signaled substrate degradation, the results of new genetic epistasis studies agree with previous genetic data in suggesting that the proteolytic activity of proteasomes is not required for error-free postreplicative repair.


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