| Summary: | 碩士 === 國立中興大學 === 生命科學系所 === 97 === Rad23 was involved in multiple functions, such as DNA repair system and ubiquitin-proteasome system. Although Rad23 was highly conserved in various species, the function regulated by signaling of Rad23 was unclear. In our lab previous data, we determined Rad23 was phosphorylated in vivo. To investigate the regulation was controlled with phosphorylated Rad23, in vitro kinase assay and immunoprepicitations were used to examine multiple positions of Rad23 were phosphrylated by Rad53 or Kin28. Rad23 mutants did not affect homo-dimerization of Rad23 itself. However, S47E mutant significantly reduced interaction with 26S subunits and multi-ubiquitin chain binding ability. In addition, S94A decreased association with Rad4 slightly. S47E also reduced contribution of Rad23 on 26S proteasome activity. In bio-function analysis, S47E increased UV light sensitivity. Based on results showed, we suggested phosphorylation of S47 within UbL domain of Rad23 might down-regulate association with 26S proteasome and survival rate with UV light stress. However, the mechanism of phosphorylated S47 would still be investigated.
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