Fasting, but Not Aging, Dramatically Alters the Redox Status of Cysteine Residues on Proteins in Drosophila melanogaster.

TitleFasting, but Not Aging, Dramatically Alters the Redox Status of Cysteine Residues on Proteins in Drosophila melanogaster.
Publication TypeJournal Article
Year of Publication2015
AuthorsMenger, KE, James, AM, Cochemé, HM, Harbour, ME, Chouchani, ET, Ding, S, Fearnley, IM, Partridge, L, Murphy, MP
JournalCell Rep
Date Published2015 Jun 17
ISSN2211-1247
Abstract

Altering the redox state of cysteine residues on protein surfaces is an important response to environmental challenges. Although aging and fasting alter many redox processes, the role of cysteine residues is uncertain. To address this, we used a redox proteomic technique, oxidative isotope-coded affinity tags (OxICAT), to assess cysteine-residue redox changes in Drosophila melanogaster during aging and fasting. This approach enabled us to simultaneously identify and quantify the redox state of several hundred cysteine residues in vivo. Cysteine residues within young flies had a bimodal distribution with peaks at ∼10% and ∼85% reversibly oxidized. Surprisingly, these cysteine residues did not become more oxidized with age. In contrast, 24 hr of fasting dramatically oxidized cysteine residues that were reduced under fed conditions while also reducing cysteine residues that were initially oxidized. We conclude that fasting, but not aging, dramatically alters cysteine-residue redox status in D. melanogaster.

DOI10.1016/j.celrep.2015.05.033
Alternate JournalCell Rep
Citation Key10.1016/j.celrep.2015.05.033
PubMed ID26095360