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Fig. 3 | Biotechnology for Biofuels and Bioproducts

Fig. 3

From: Harnessing redox proteomics to study metabolic regulation and stress response in lignin-fed Rhodococci

Fig. 3

Overview of the differentially oxidized protein at cysteine site level (p-value < 0.05, and fold-change ≥ 1.5) among the lysate samples from glucose or lignin fermentation after 5 days. The ID prefixes correspond to the following: “Pd630” = R. opacus PD630 and “26,252…” = R. jostii RHA1. Left panel: protein abundance level; right panel: protein cysteine thiol oxidation level. Relative abundances (intensities) of proteins or HPE-IAM-Cys peptides were log2 transformed and median centered to zero. Each row represents one protein Cys site and each column represented one sample. “G1”, “G2” and “G3” are the lysate triplicate samples from glucose fermentation; “L1”, “L2” and “L3” are the lysate triplicate samples from lignin fermentation. All the fermentation was conducted by co-culture of three strains: R. jostii RHA1, R. jostii RHA1 vanAR. opacus PD630. The protein name abbreviation was followed by FASTA IDs of strains and Cys site IDs. A The selected proteins more oxidized during lignin fermentation. B The selected proteins more reduced during lignin fermentation

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