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

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.

journal_name

Cell Rep

journal_title

Cell reports

authors

Menger KE,James AM,Cochemé HM,Harbour ME,Chouchani ET,Ding S,Fearnley IM,Partridge L,Murphy MP

doi

10.1016/j.celrep.2015.05.033

subject

Has Abstract

pub_date

2015-06-30 00:00:00

pages

1856-65

issue

12

issn

2211-1247

pii

S2211-1247(15)00569-0

journal_volume

11

pub_type

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