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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

The DNA repair protein rad23 is a negative regulator of multi-ubiquitin chain assembly.

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 rad23Delta 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.[1]

References

  1. The DNA repair protein rad23 is a negative regulator of multi-ubiquitin chain assembly. Ortolan, T.G., Tongaonkar, P., Lambertson, D., Chen, L., Schauber, C., Madura, K. Nat. Cell Biol. (2000) [Pubmed]
 
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