tpj12310-sup-0009-Legends

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LEGENDS to Supplemental Figures
Figure S1. Transcript levels of six cytochrome c oxidase related genes. Data are the
means ± SD from six independent experiments. The levels were calibrated relative to
the value obtained in the GT strain under nitrogen-replete conditions, which was set at
100%. Differences between GT and GOX50 analysed using Student’s t-test were
statistically significant (*P<0.05).
Figure S2. Transcript levels of genes encoding PSII core proteins. Data are the mean ±
SD from six independent experiments. The levels were calibrated relative to the value
obtained in the GT strain under nitrogen-replete conditions, which was set at 100%.
Differences between GT and GOX50 analysed using Student’s t-test were statistically
significant (*P<0.05, **P<0.005).
Figure S3. Transcript levels of genes encoding PSII peripheral or small accessory
proteins. Data are the mean ± SD from six independent experiments. The levels were
calibrated relative to the value obtained in the GT strain under nitrogen-replete
conditions, which was set at 100%. Differences between GT and GOX50 analysed using
Student’s t-test were statistically significant (*P<0.05, **P<0.005).
Figure S4. Transcript levels of genes encoding PSII oxygen-evolving complex proteins.
Data are the mean ± SD from six independent experiments. The levels were calibrated
relative to the value obtained in the GT strain under nitrogen-replete conditions, which
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was set at 100%. Differences between GT and GOX50 analyzed using Student’s t-test
were statistically significant (*P<0.05, **P<0.005).
Figure S5. Transcript levels of genes encoding PSI proteins. Data are the mean ± SD
from independent experiments (n = 4–6). The levels were calibrated relative to the value
obtained in the GT strain under nitrogen-replete conditions, which was set at 100%.
Differences between GT and GOX50 analysed using Student’s t-test were statistically
significant (*P<0.05, **P<0.005).
Figure S6. Levels of PsbA, PsbO, and PsaD proteins. Total protein 12 g was subjected
to immunoblotting. Data are the mean ± SD from three independent experiments. The
expression levels were calibrated relative to the value obtained in the GT strain under
nitrogen-replete conditions, which was set at 100%. Differences between GT and
GOX50 analysed using Student’s t-test were statistically significant (*P<0.05).
Figure S7. Levels of Rre12, Rre37, and PII proteins. (A) Purification of
histidine-tagged Rre12. Histidine-tagged Rre12 (His-Rre12) purified from insoluble
fraction of E. coli was subjected by SDS-PAGE and Coomassie brilliant blue staining.
FT indicates flow-through fraction containing proteins unbound to resins. (B) Total
protein (12 g for Rre12 and Rre37 or 6 g for PII) was subjected to immunoblotting.
Data represent means ±SD of values from four independent experiments. Expression
levels were calibrated relative to that in GT strain under nitrogen-replete conditions (for
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PII) or nitrogen-depleted conditions after nitrogen depletion (for Rre12 and Rre37),
which were set at 100%. Asterisks indicate significant differences between GT and
GOX50 analysed using Student’s t-test (*P<0.05, **P<0.005).
Figure S8. Levels of ChlH and SigA proteins. Total protein (12 g) was subjected to
immunoblotting. Data represent means ±SD of values from four independent
experiments. ChlI protein levels are shown as loading control. Expression levels were
calibrated relative to that in GT strain under nitrogen-replete conditions, which was set
at 100%. Asterisk indicates significant difference between GT and GOX50 analysed
using Student’s t-test (*P<0.05).
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