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Quantitative proteomic analysis of the rice (Oryza sativa L.) salt response.

Xu J, Lan H, Fang H, Huang X, Zhang H, Huang J - PLoS ONE (2015)

Bottom Line: Moreover, physiological data including total antioxidant capacity, peroxiredoxin activity, chlorophyll a/b content, glutathione S-transferase activity, reduced glutathione content and ATPase activity were consistent with changes in the levels of these proteins.The levels of the mRNAs encoding these proteins were also analyzed by real-time quantitative reverse transcription PCR, and approximately 86% of the results were consistent with the iTRAQ data.This study provides information for an improved understanding of the function of photosynthesis and PSI in the salt-stress response of rice.

View Article: PubMed Central - PubMed

Affiliation: State key laboratory of crop genetics and germplasm enhancement, Nanjing Agricultural University, Nanjing, 210095, China; Jiangsu Collaborative Innovation Center for Modern Crop Production, Nanjing, 210095, China.

ABSTRACT
Salt stress is one of most serious limiting factors for crop growth and production. An isobaric Tags for Relative and Absolute Quantitation (iTRAQ) approach was used to analyze proteomic changes in rice shoots under salt stress in this study. A total of 56 proteins were significantly altered and 16 of them were enriched in the pathways of photosynthesis, antioxidant and oxidative phosphorylation. Among these 16 proteins, peroxiredoxin Q and photosystem I subunit D were up-regulated, while thioredoxin M-like, thioredoxin x, thioredoxin peroxidase, glutathione S-transferase F3, PSI subunit H, light-harvesting antenna complex I subunits, chloroplast chaperonin, vacuolar ATP synthase subunit H, and ATP synthase delta chain were down-regulated. Moreover, physiological data including total antioxidant capacity, peroxiredoxin activity, chlorophyll a/b content, glutathione S-transferase activity, reduced glutathione content and ATPase activity were consistent with changes in the levels of these proteins. The levels of the mRNAs encoding these proteins were also analyzed by real-time quantitative reverse transcription PCR, and approximately 86% of the results were consistent with the iTRAQ data. Importantly, our data suggest the important role of PSI in balancing energy supply and ROS generation under salt stress. This study provides information for an improved understanding of the function of photosynthesis and PSI in the salt-stress response of rice.

No MeSH data available.


Related in: MedlinePlus

The differentially expressed proteins involved in photosynthesis.Transcript abundances of mRNAs encoding proteins involved in photosynthesis were analyzed at 0 h, 1 h, 3 h, 6 h, 12 h and 24 h following salt stress treatment. The mRNA levels at 12 h were compared with the iTRAQ data. Red indicates the proteins that were up-regulated while green indicates the proteins that were down-regulated. Significant differences were determined relative to each treatment using a student’s t-test [P-values <0.05 (*) and <0.01 (**)]. Bars: SD. The changes in transcript abundances at 12 h were compared with the iTRAQ data. (A) Putative PSI antenna protein (Lhca2, gi/34393511). (B) Chlorophyll a/b-binding protein precursor (Lhca1, gi/3789954). (C) Chlorophyll a/b-binding protein precursor (Lhca4, gi/3789952). (D) Chloroplast photosystem I reaction center subunit II precursor-like protein (PsaD, gi/29367391). (E) PSI H subunit GOS5 (PsaH, gi/3885894). (F) Overview of the differentially expressed proteins involved in photosynthesis.
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pone.0120978.g003: The differentially expressed proteins involved in photosynthesis.Transcript abundances of mRNAs encoding proteins involved in photosynthesis were analyzed at 0 h, 1 h, 3 h, 6 h, 12 h and 24 h following salt stress treatment. The mRNA levels at 12 h were compared with the iTRAQ data. Red indicates the proteins that were up-regulated while green indicates the proteins that were down-regulated. Significant differences were determined relative to each treatment using a student’s t-test [P-values <0.05 (*) and <0.01 (**)]. Bars: SD. The changes in transcript abundances at 12 h were compared with the iTRAQ data. (A) Putative PSI antenna protein (Lhca2, gi/34393511). (B) Chlorophyll a/b-binding protein precursor (Lhca1, gi/3789954). (C) Chlorophyll a/b-binding protein precursor (Lhca4, gi/3789952). (D) Chloroplast photosystem I reaction center subunit II precursor-like protein (PsaD, gi/29367391). (E) PSI H subunit GOS5 (PsaH, gi/3885894). (F) Overview of the differentially expressed proteins involved in photosynthesis.

Mentions: Six differentially expressed proteins were involved in photosynthesis (Table 1, Fig. 3). Among three light-harvesting antenna complex I (LHCI) subunits, levels of the light-harvesting complex I subunit 1 (Lhca1) precursor, putative Lhca2 and Lhca4 precursors were reduced by 41.9%, 36.5% and 45.1% under salt stress treatment, respectively. The PSI subunit D (PsaD) precursor, chloroplast PSI reaction center subunit II precursor-like protein, was increased by 1.585-fold, while the levels of the PSI H subunit GOS5 reduced by 37.6%. The level of the putative chloroplast chaperonin was decreased by 34.9%. These proteins were only involved in PSI (S4 Fig.), and no protein organizing the PSII complex was found differently expressed in our data.


Quantitative proteomic analysis of the rice (Oryza sativa L.) salt response.

Xu J, Lan H, Fang H, Huang X, Zhang H, Huang J - PLoS ONE (2015)

The differentially expressed proteins involved in photosynthesis.Transcript abundances of mRNAs encoding proteins involved in photosynthesis were analyzed at 0 h, 1 h, 3 h, 6 h, 12 h and 24 h following salt stress treatment. The mRNA levels at 12 h were compared with the iTRAQ data. Red indicates the proteins that were up-regulated while green indicates the proteins that were down-regulated. Significant differences were determined relative to each treatment using a student’s t-test [P-values <0.05 (*) and <0.01 (**)]. Bars: SD. The changes in transcript abundances at 12 h were compared with the iTRAQ data. (A) Putative PSI antenna protein (Lhca2, gi/34393511). (B) Chlorophyll a/b-binding protein precursor (Lhca1, gi/3789954). (C) Chlorophyll a/b-binding protein precursor (Lhca4, gi/3789952). (D) Chloroplast photosystem I reaction center subunit II precursor-like protein (PsaD, gi/29367391). (E) PSI H subunit GOS5 (PsaH, gi/3885894). (F) Overview of the differentially expressed proteins involved in photosynthesis.
© Copyright Policy
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC4368772&req=5

pone.0120978.g003: The differentially expressed proteins involved in photosynthesis.Transcript abundances of mRNAs encoding proteins involved in photosynthesis were analyzed at 0 h, 1 h, 3 h, 6 h, 12 h and 24 h following salt stress treatment. The mRNA levels at 12 h were compared with the iTRAQ data. Red indicates the proteins that were up-regulated while green indicates the proteins that were down-regulated. Significant differences were determined relative to each treatment using a student’s t-test [P-values <0.05 (*) and <0.01 (**)]. Bars: SD. The changes in transcript abundances at 12 h were compared with the iTRAQ data. (A) Putative PSI antenna protein (Lhca2, gi/34393511). (B) Chlorophyll a/b-binding protein precursor (Lhca1, gi/3789954). (C) Chlorophyll a/b-binding protein precursor (Lhca4, gi/3789952). (D) Chloroplast photosystem I reaction center subunit II precursor-like protein (PsaD, gi/29367391). (E) PSI H subunit GOS5 (PsaH, gi/3885894). (F) Overview of the differentially expressed proteins involved in photosynthesis.
Mentions: Six differentially expressed proteins were involved in photosynthesis (Table 1, Fig. 3). Among three light-harvesting antenna complex I (LHCI) subunits, levels of the light-harvesting complex I subunit 1 (Lhca1) precursor, putative Lhca2 and Lhca4 precursors were reduced by 41.9%, 36.5% and 45.1% under salt stress treatment, respectively. The PSI subunit D (PsaD) precursor, chloroplast PSI reaction center subunit II precursor-like protein, was increased by 1.585-fold, while the levels of the PSI H subunit GOS5 reduced by 37.6%. The level of the putative chloroplast chaperonin was decreased by 34.9%. These proteins were only involved in PSI (S4 Fig.), and no protein organizing the PSII complex was found differently expressed in our data.

Bottom Line: Moreover, physiological data including total antioxidant capacity, peroxiredoxin activity, chlorophyll a/b content, glutathione S-transferase activity, reduced glutathione content and ATPase activity were consistent with changes in the levels of these proteins.The levels of the mRNAs encoding these proteins were also analyzed by real-time quantitative reverse transcription PCR, and approximately 86% of the results were consistent with the iTRAQ data.This study provides information for an improved understanding of the function of photosynthesis and PSI in the salt-stress response of rice.

View Article: PubMed Central - PubMed

Affiliation: State key laboratory of crop genetics and germplasm enhancement, Nanjing Agricultural University, Nanjing, 210095, China; Jiangsu Collaborative Innovation Center for Modern Crop Production, Nanjing, 210095, China.

ABSTRACT
Salt stress is one of most serious limiting factors for crop growth and production. An isobaric Tags for Relative and Absolute Quantitation (iTRAQ) approach was used to analyze proteomic changes in rice shoots under salt stress in this study. A total of 56 proteins were significantly altered and 16 of them were enriched in the pathways of photosynthesis, antioxidant and oxidative phosphorylation. Among these 16 proteins, peroxiredoxin Q and photosystem I subunit D were up-regulated, while thioredoxin M-like, thioredoxin x, thioredoxin peroxidase, glutathione S-transferase F3, PSI subunit H, light-harvesting antenna complex I subunits, chloroplast chaperonin, vacuolar ATP synthase subunit H, and ATP synthase delta chain were down-regulated. Moreover, physiological data including total antioxidant capacity, peroxiredoxin activity, chlorophyll a/b content, glutathione S-transferase activity, reduced glutathione content and ATPase activity were consistent with changes in the levels of these proteins. The levels of the mRNAs encoding these proteins were also analyzed by real-time quantitative reverse transcription PCR, and approximately 86% of the results were consistent with the iTRAQ data. Importantly, our data suggest the important role of PSI in balancing energy supply and ROS generation under salt stress. This study provides information for an improved understanding of the function of photosynthesis and PSI in the salt-stress response of rice.

No MeSH data available.


Related in: MedlinePlus