(A) represents the numbers of peptides identified from samples with different treatments: 10-min H2O2 treatment (a), 10-min deionized water treatment (b), 15-min white light treatment (c), and 15-min UV-B treatment (d). Index 1, 2 and 3 in circle represents the peptides detected in reduced (MPB-labeled), oxidized (BIAM-labeled) and both reduced and oxidized (both MPB- and BIAM-labeled) forms, respectively.
(B) shows the redox state changes of two independent redox-sensitive cysteine-containing peptides from both MPB- and BIAM-labeled experiments. 85YYCTVIDAPGHR and 172SFQCELVMAK is derived from GTP binding Elongation factor Tu family proteins (AT1G07920, AT1G07930, AT1G07940 or AT5G60390) and RuBisCO activase (RCA, AT2G39730), respectively.
(C) and (D) represents the 3-D structure of aa2~aa431 region of GTP binding Elongation factor Tu family protein (AT1G07920) and aa123~aa415 region of RCA, respectively. The structures are depicted by ESyPred3D program, in which all cysteine residues are highlighted with the colored atoms: Green stands for carbon, red for oxygen, blue for nitrogen and yellow for sulfur, respectively. Cysteines reduced by 15-min UV-B exposure, i.e. C87 of GTP binding Elongation factor Tu family protein (AT1G07920) and C175 of RCA, are annotated in red. The distances between these two residues and their closest cysteines are indicated, with which the intra-molecular disulfide bridges may form between the sulfide atoms linked by blue bars when conformation changes.
