Identification of substrates of F-box protein involved in methylmercury toxicity in yeast cells

Jin Yong Lee, Yosuke Ishida, Shusuke Kuge, Akira Naganuma, Gi Wook Hwang

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


We previously reported that some of the substrate proteins recognized by Hrt3 or Ucc1, a component of Skp1/Cdc53/F-box protein ubiquitin ligase, may include proteins that are involved in the methylmercury toxicity and degraded by the proteasome. In this study, we found that Dld3 and Grs1 bound to Hrt3 and that Eno2 bound to Ucc1 using a yeast two-hybrid screening. We demonstrated that Dld3 and Grs1 are substrates that are ubiquitinated by Hrt3, and Eno2 is a substrate that is ubiquitinated by Ucc1. Moreover, any yeast showing overexpression of Dld3, Grs1, and Eno2 demonstrated higher methylmercury sensitivity. This indicates that Hrt3 and Ucc1 are involved in alleviating the methylmercury toxicity by promoting proteasomal degradation through the ubiquitination of Dld3, Grs1, and Eno2.

Original languageEnglish
Pages (from-to)2720-2725
Number of pages6
JournalFEBS Letters
Issue number19
Publication statusPublished - 2015 Sep 14


  • F-box protein
  • Methylmercury
  • Toxicity
  • Ubiquitination

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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