Fig. 8
From: The identification of carbon dioxide mediated protein post-translational modifications
Biochemical validation of AtPRX34 as a carbamylated protein. a MSMS spectra of peptides containing ethyl-trapped carbamates on Lys 262 and Lys 268 of At3g49120. The peptide sequences above the panel indicate the assignment of predominantly singly charged y (red) and b (blue) ions. The modified residue is indicated in bold. Kcarb.Et indicates the molecular weight difference between ions diagnostic of the modified Lys. b The ratios of the specific activities of wild type, K262A or K268A AtPRX34 protein at atmospheric CO2 or in the absence of CO2 (* p < 0.0001 compared to wild type, one-way ANOVA with Dunn Bonferroni multiple comparison test, n = 12 independent replicates, Kruskal–Wallis statistic = 26.4, ±S.D.; ** p < 0.0028 compared to wild type, one-way ANOVA with Dunn Bonferroni multiple comparison test, n = 12 independent replicates, Kruskal-Wallis statistic = 26.4, ±S.D.). Inset—purification of recombinant AtPRX34 proteins (1.0 μg; SDS/PAGE analysis and Coomassie Blue staining). c The ratios of the specific activities of wild type, K262E or K268E AtPRX34 protein at atmospheric CO2 or in the absence of CO2 (* p < 0.0001 compared to wild type, one-way ANOVA with Dunn Bonferroni multiple comparison test, n = 9 independent replicates, Kruskal–Wallis statistic = 19.53, ±S.D.; ** p < 0.0194 compared to wild type, one-way ANOVA with Dunn Bonferroni multiple comparison test, n = 9 independent replicates, Kruskal–Wallis statistic = 19.53, ±S.D.). Inset- Purification of recombinant PRX34 proteins (1.0 μg; SDS/PAGE analysis and Coomassie Blue staining)
