SUPPLEMENTARY DATA Table S1: Minimal dye labeling setup of 2D-DIGE experiments using Cy2, Cy3 and Cy5. Internal standard contained an equal amount of each sample. Three biological replicates were conducted. Gel no Time point (day) Cy2 Cy3 Cy5 1 4 Pooled internal standard Untreated Drought- treated 2 4 Pooled internal standard Drought- treated Untreated 3 4 Pooled internal standard Untreated Drought- treated 1 8 Pooled internal standard Untreated Drought- treated 2 8 Pooled internal standard Drought- treated Untreated 3 8 Pooled internal standard Untreated Drought- treated 1 12 Pooled internal standard Untreated Drought- treated 2 12 Pooled internal standard Drought- treated Untreated 3 12 Pooled internal standard Untreated Drought- treated

static-content.springer.com10.1007... · Web view500 µg protein were separated on a 17 cm, pH 3-10 nonlinear strip, followed by separation on 12% SDS-PAGE gel. Fig. S2: STRING analysis

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Page 1: static-content.springer.com10.1007... · Web view500 µg protein were separated on a 17 cm, pH 3-10 nonlinear strip, followed by separation on 12% SDS-PAGE gel. Fig. S2: STRING analysis

SUPPLEMENTARY DATA

Table S1: Minimal dye labeling setup of 2D-DIGE experiments using Cy2, Cy3 and Cy5. Internal standard contained an equal amount of each sample. Three biological replicates were conducted.

Gel no Time point (day) Cy2 Cy3 Cy5

1 4 Pooled internal standard Untreated Drought-treated

2 4 Pooled internal standard Drought-treated Untreated

3 4 Pooled internal standard Untreated Drought-treated

1 8 Pooled internal standard Untreated Drought-treated

2 8 Pooled internal standard Drought-treated Untreated

3 8 Pooled internal standard Untreated Drought-treated

1 12 Pooled internal standard Untreated Drought-treated

2 12 Pooled internal standard Drought-treated Untreated

3 12 Pooled internal standard Untreated Drought-treated

Page 2: static-content.springer.com10.1007... · Web view500 µg protein were separated on a 17 cm, pH 3-10 nonlinear strip, followed by separation on 12% SDS-PAGE gel. Fig. S2: STRING analysis

Fig. S1: Coomassie blue stained preparative gel of pooled Brachypodium samples. 500 µg protein were separated on a 17 cm, pH 3-10 nonlinear strip, followed by separation on 12% SDS-PAGE gel.

Page 3: static-content.springer.com10.1007... · Web view500 µg protein were separated on a 17 cm, pH 3-10 nonlinear strip, followed by separation on 12% SDS-PAGE gel. Fig. S2: STRING analysis

Fig. S2: STRING analysis revealing close interaction partners of identified proteins in this study. Different line colors represent the types of functional link. BRADI1G58160.1: Oxygen-evolving enhancer protein 2, BRADI1G56580.1: Oxygen-evolving enhancer protein 1, BRADI5G07190.1: Transketolase, BRADI4G24367.1: Aldolase, BRADI5G09650.1: 2-cys peroxiredoxin, BRADI4G39470.1: Stromal HSP70, BRADI1G69680.1: Superoxide dismutase, BRADI5G05900.1: Mitochondrial HSP70, BRADI2G44856.1: Carbonic anhydrase, BRADI3G14120.3: Glyceraldehyde-3-phosphate dehydrogenase, BRADI1G09300.2: Serine hydroxymethyl transferase, BRADI4G09120.2: Rubisco activase B, BRADI3G26391.2: Rubisco small subunit, BRADI2G21120.1: Phosphoglycerate kinase chloroplastic-like, BRADI3G05220.1: Phosphoglycerate kinase cytosolic-like, BRADI2G59370.1: Transaldolase, BRADI3G27600.1: Phosphoglycerate kinase like, BRADI4G07810.1: Bifunctional dihydrofolate reductase-thymidylate synthase-like. Known interactions are represented as blue (from curated databases) and pink (experimentally determined) nodes. Other colors represents predicted interactions.