Oxidative stress studies in yeast with a frataxin mutant: A proteomics perspective

Jin Hee Kim, Miroslav Sedlak, Qiang Gao, Catherine P. Riley, Fred E. Regnier, Jiri Adamec

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


Cellular response of wild-type Saccharomyces cerevisiae and the Δyfh1 mutant to oxidative stress (OS) was examined by stressing cells through the addition of H2O2 to the growth medium. The Δyfh1 mutant is unusual in that it accumulates iron in it is mitochondria. Wild-type growth was immediately arrested and recovered in 2 h following H 2O2 treatment. No change in viability was observed. Growth of the mutant, on the other hand, was similar to wild-type yeast for 4 h but then rapidly declined, eventually reaching zero. Levels of carbonyl groups and reactive oxygen species (ROS) reached their maximum at 3 h following exposure. The impact of OS on protein function was also evaluated by proteomic techniques targeting protein carbonylation. Oxidized proteins were selected by affinity chromatography, and following trypsin digestion, peptide fragments were identified by RPLC-MS/MS. A total of 53 proteins were identified in both wild-type and mutant cells, respectively.

Original languageEnglish (US)
Pages (from-to)730-736
Number of pages7
JournalJournal of proteome research
Issue number2
StatePublished - Feb 5 2010
Externally publishedYes


  • Cell viability
  • Frataxin
  • Friedreich ataxia
  • Oxidative stress
  • Protein damage

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)


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