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Le Moan N, et al.  (2006) The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways. J Biol Chem 281(15):10420-30

Abstract: Protein-thiol oxidation subserves important biological functions and constitutes a sequel of ROS toxicity. We developed two distinct thiol-labeling approaches to identify oxidized cytoplasmic protein-thiol in S. cerevisiae. One used Biotin-HPDP to purify oxidized protein-thiols and the other 14C-NEM to quantify this oxidation. Both approaches showed a large number of same proteins with oxidized thiols (about 200), of which sixty-four were identified by mass spectrometry. We show that, irrespective of its mechanism, protein-thiol oxidation is dependent upon molecular O2. We also show that H2O2 does not cause de novo protein-thiol oxidation but rather increases the oxidation state of a select group of proteins. Further, our study reveals contrasted differences in the oxidized proteome of cells with inactivation of the thioredoxin or GSH pathways suggestive of very distinct thiol-redox control functions, assigning an exclusive role for thioredoxin in H2O2 metabolism and the presumed thiol-redox buffer function for GSH. Taken together, these results suggest the high selectivity of cytoplasmic protein-thiol oxidation.

Status: Published Type: Journal Article PubMed ID: 16418165

Topics addressed in this paper

Number of different genes curated to this paper: 68

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ACO1 ADH1 ADO1 AHP1 ALD6 ASC1 CCS1 CDC19 CDC48 CPR1
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CPR6 CYS4 EFB1 ENO1 ENO2 FBA1 GDH1 GLR1 GPX2 GSH1
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GSP1 GUK1 HOM2 HSP60 HXK2 HYP2 ILV5 IPP1 LEU1 MDH1
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Topics Genes linked to topics (#31 - 40 )
MET17 MET6 MXR1 PDC1 PDI1 PEP4 PGK1 PMI40 POR1 PRX1
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PSA1 RHR2 RPL12A RPS0A RPS5 SAM1 SAM2 SEC53 SHM2 SOD1
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SSA2 SSB1 SSE1 STI1 TDH3 TEF1 TKL1 TMA19 TPI1 TRR1
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Topics Genes linked to topics (#61 - 68 )
TRX1 TRX2 TSA1 TSA2 UBC1 UBC4 URA1 YHB1
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