Journal
NATURE CELL BIOLOGY
Volume 2, Issue 9, Pages 601-608Publisher
MACMILLAN PUBLISHERS LTD
DOI: 10.1038/35023547
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Funding
- NIGMS NIH HHS [GM-RO1-52058] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM052058] Funding Source: NIH RePORTER
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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 cc-precipitated with a substrate that contained a short multi-Ub chain. The UV sensitivity of rad23 Delta was reduced in mutants lacking the E2 enzyme Ubc4, or the multi-Db chain-promoting factor Ufd2, These studies suggest that the stability of proteolytic substrates is governed by the competing action of multi-Db chain-promoting and chain-inhibiting factors. The stabilization of DNA repair and stress factors could represent an important biological function of Rad23.
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