Author: ["Tatiana G. Ortolan","Prasad Tongaonkar","David Lambertson","Li Chen","Cherylene Schauber","Kiran Madura"]
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Abstract
Rad23 is a nucleotide-excision repair protein with a previously unknown biochemical function. We determined that yeast and human Rad23 inhibited multi-ubiquitin (Ub) chain formation and the degradation of proteolytic substrates. Significantly, Rad23 could be co-precipitated with a substrate that contained a short multi-Ub chain. The UV sensitivity of rad23Δ was reduced in mutants lacking the E2 enzyme Ubc4, or the multi-Ub chain-promoting factor Ufd2. These studies suggest that the stability of proteolytic substrates is governed by the competing action of multi-Ub chain-promoting and chain-inhibiting factors. The stabilization of DNA repair and stress factors could represent an important biological function of Rad23.Cite this article
Ortolan, T., Tongaonkar, P., Lambertson, D. et al. The DNA repair protein Rad23 is a negative regulator of multi-ubiquitin chain assembly. Nat Cell Biol 2, 601–608 (2000). https://doi.org/10.1038/35023547 