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• W2017386314 abstract "Rad23 is a DNA repair protein that promotes the assembly of the nucleotide excision repair complex. Rad23 can interact with the 26S proteasome through an N-terminal ubiquitin-like domain, and inhibits the assembly of substrate-linked multi-ubiquitin (multi-Ub) chains in vitro and in vivo. Significantly, Rad23 can bind a proteolytic substrate that is conjugated to a few ubiquitin (Ub) moieties. We report here that two ubiquitin-associated (UBA) domains in Rad23 form non-covalent interactions with Ub. A mutant that lacked either UBA sequence was capable of blocking the assembly of substrate-linked multi-Ub chains, although a mutant that lacked both UBA domains was significantly impaired. These studies suggest that the interaction with Ub is required for Rad23 activity, and that other UBA-containing proteins may have a similar function." @default.
• W2017386314 created "2016-06-24" @default.
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• W2017386314 date "2001-10-01" @default.
• W2017386314 modified "2023-10-11" @default.
• W2017386314 title "Ubiquitin‐associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi‐ubiquitin chain assembly" @default.
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• W2017386314 doi "https://doi.org/10.1093/embo-reports/kve203" @default.
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