Proteomic analysis of the effect of heat stress on hexaploid wheat grain: Characterization of heat‐responsive proteins from non‐prolamins fraction

Majoul, Thouraya; Bancel, Emmanuelle; Triboı̈, E.; Hamida, Jeannette Ben; Branlard, Gérard

doi:10.1002/pmic.200300570

Cited by 188 publications

(116 citation statements)

References 43 publications

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“…ATP synthase, a multisubunit complex that spans the inner membrane, is the main enzyme of the ATP biosynthetic pathway. The catalytic site for ATP synthesis is localized primarily on the beta-subunit; ATP is produced from ADP in the presence of a proton gradient across the Mt membrane and a decrease in the amount of ATP synthase may affect energy-dependent processes involved in heat stress resistance [12]. Taken together, these results suggest that the energy production systems of plants are highly affected by heat stress and increases of the chloroplastidal F1 alpha subunit possibly re-establish this system.…”

Section: Energy and Metabolismsmentioning

confidence: 89%

“…The current status of rice proteomic analysis has been reviewed recently [10], but there still are no reports regarding the effects of heat stress on rice leaves. Thus far, there have been only a few proteomic studies regarding heat stress in plants [3,5,[11][12][13]. To the best of our knowledge, only one proteomic analysis has been carried out during the caryopsis development of rice under heat stress [3].…”

Section: Introductionmentioning

confidence: 99%

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A proteomic approach in analyzing heat‐responsive proteins in rice leaves

et al. 2007

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The present study investigated rice leaf proteome in response to heat stress. Rice seedlings were subjected to a temperature of 427C and samples were collected 12 and 24 h after treatment. Increased relative ion leakage and lipid peroxidation suggested that oxidative stress frequently was generated in rice leaves exposed to high temperature. 2-DE, coupled with MS, was used to investigate and identify heat-responsive proteins in rice leaves. In order to identify the low-abundant proteins in leaves, samples were prefractionated by 15% PEG. The PEG supernatant and the pellet fraction samples were separated by 2-DE, and visualized by silver or CBB staining. Approximately 1000 protein spots were reproducibly detected on each gel, wherein 73 protein spots were differentially expressed at least at one time point. Of these differentially expressed proteins, a total of 34 and 39 protein spots were found in the PEG supernatant and pellet fractions, respectively. Using MALDI-TOF MS, a total of 48 proteins were identified. These proteins were categorized into classes related to heat shock proteins, energy and metabolism, redox homeostasis, and regulatory proteins. The results of the present study show that a group of low molecular small heat shock proteins (sHSPs) were newly induced by heat stress. Among these sHSPs, a low molecular weight mitochondrial (Mt) sHSP was validated further by Western blot analysis. Furthermore, four differentially accumulated proteins that correspond to antioxidant enzymes were analyzed at the mRNA level, which confirmed the differential gene expression levels, and revealed that transcription levels were not completely concomitant with translation. The identification of some novel proteins in the heat stress response provides new insights that can lead to a better understanding of the molecular basis of heat-sensitivity in plants.

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Section: Energy and Metabolismsmentioning

confidence: 89%

Section: Introductionmentioning

confidence: 99%

A proteomic approach in analyzing heat‐responsive proteins in rice leaves

et al. 2007

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“…When comparing results on Chlamydomonas with proteomics studies conducted on various land plants (Skylas et al, 2002;Majoul et al, 2003Majoul et al, , 2004Süle et al, 2004;Ferreira et al, 2006;Lee et al, 2007;Palmblad et al, 2008;Valcu et al, 2008;Xu and Huang, 2008;Scafaro et al, 2010;Xu and Huang, 2010), we concluded that the upregulation of chaperones, FKBP65 orthologs, and thiamine biosynthesis protein and the downregulation of ferredoxin-NADP(H) oxidoreductase, Rubisco, methionine synthase, adenosylhomocysteinase, and S-adenosylmethionine synthetase are conserved in the green lineage. However, there were also many inconsistencies between these studies.…”

Section: Introductionmentioning

confidence: 99%

Systems-Wide Analysis of Acclimation Responses to Long-Term Heat Stress and Recovery in the Photosynthetic Model OrganismChlamydomonas reinhardtii

et al. 2014

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We applied a top-down systems biology approach to understand how Chlamydomonas reinhardtii acclimates to long-term heat stress (HS) and recovers from it. For this, we shifted cells from 25 to 42°C for 24 h and back to 25°C for ‡8 h and monitored abundances of 1856 proteins/protein groups, 99 polar and 185 lipophilic metabolites, and cytological and photosynthesis parameters. Our data indicate that acclimation of Chlamydomonas to long-term HS consists of a temporally ordered, orchestrated implementation of response elements at various system levels. These comprise (1) cell cycle arrest; (2) catabolism of larger molecules to generate compounds with roles in stress protection; (3) accumulation of molecular chaperones to restore protein homeostasis together with compatible solutes; (4) redirection of photosynthetic energy and reducing power from the Calvin cycle to the de novo synthesis of saturated fatty acids to replace polyunsaturated ones in membrane lipids, which are deposited in lipid bodies; and (5) when sinks for photosynthetic energy and reducing power are depleted, resumption of Calvin cycle activity associated with increased photorespiration, accumulation of reactive oxygen species scavengers, and throttling of linear electron flow by antenna uncoupling. During recovery from HS, cells appear to focus on processes allowing rapid resumption of growth rather than restoring pre-HS conditions.

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“…The albumin and globulin fractions represent about 9 and 5% of wheat seed proteins, respectively, and they are mainly present in embryo and aleurone (Singh and Skerritt 2001). The molecular weights of albumins and globulins are mostly between 12 to 60 kD, with the high molecular weight (HMW) albumins in the range of 45Á65 kD and triticins 22Á58 kD (Singh and Skerritt 2001;Bean and Tilley 2003;Majoul et al 2004). In some cases, HMW albumins and triticins are storage proteins, which have the characteristics of wheat storage proteins Shepherd 1985, 1987;Gupta et al 1991).…”

mentioning

confidence: 99%

“…Mots clé s: Triticum aestivum, ble´tendre, prote´ines hydrosolubles, e´lectrophore`se capillaire, marqueurs biochimiques Wheat grain proteins are classified into two major groups: the main storage proteins of the endosperm (gliadins and glutenins) called prolamins, and the nonprolamins consisting of water-soluble (WS) albumins and salt-soluble globulins (Majoul et al 2004). The albumin and globulin fractions represent about 9 and 5% of wheat seed proteins, respectively, and they are mainly present in embryo and aleurone (Singh and Skerritt 2001).…”

mentioning

confidence: 99%

Rapid separation and characterization of grain water-soluble proteins in bread wheat cultivars (Triticum aestivum L.) by capillary electrophoresis

Wang¹,

Pei²,

Li³

et al. 2008

Can. J. Plant Sci.

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. 2008. Rapid separation and characterization of grain water-soluble proteins in bread wheat cultivars (Triticum aestivum L.) by capillary electrophoresis. Can. J. Plant Sci. 88: 843Á848. Water-soluble (WS) proteins in wheat grain are considered to represent the suite of biologically active enzymes and enzyme inhibitors in the grain. In this study, a rapid capillary electrophoresis (CE) method for WS protein separations was developed using untreated fused-silica columns and an acidic phosphate-glycine buffer system. In order to optimize the resolution and reproducibility of CE separation, different protein extraction methods, organic modifiers in phosphate-glycine buffer and capillary electrophoresis conditions, including capillary length and inner diameter (ID), operating temperature, performance voltages, sample injection times, etc., were investigated. High resolution and reproducibility of WS proteins were achieved using 20% ethanol as the extracting buffer. The optimal condition to separate these proteins was 50 mm ID)31.5 cm (26.5 cm to the detector) capillary at 11.0 kV and 358C. The optimum buffer was 0.1 M phosphate-glycine (pH 2.5) containing 20% acetonitrile (ACN) and 0.05% hydroxylpropylmethylcellulose. Using this method, the WS proteins were well separated in less than 10 min. A total of 120 Chinese bread wheat cultivars were analyzed. The CE patterns of most bread wheat cultivars showed a higher level of polymorphisms compared with SDS-PAGE patterns. All cultivars analyzed could be readily differentiated based on their WS protein profiles. Results indicate that the WS proteins are useful biochemical markers for wheat genetics and breeding research and CE is expected to become a new and powerful tool for the separation and characterization of grain WS proteins in bread wheat.Key words: Triticum aestivum, bread wheat, water-soluble proteins, capillary electrophoresis, biochemical markers Wang, A., Pei, Y., Li, X., Zhang, Y., Zhang, Q., He, Z., Xia, X., Appels, R., Ma, W., Huang, X.-Q. et Yan, Y. 2008. Se´paration et caracte´risation rapides des prote´ines hydrosolubles dans le grain des cultivars de ble´tendre (Triticum aestivum L.) par e´lectrophore`se capillaire. Can. J. Plant Sci. 88: 843Á848. Les prote´ines hydrosolubles, estime-t-on, correspondent al 'ensemble des enzymes biologiquement actives et des inhibiteurs des enzymes pre´sents dans le grain du ble´tendre. Les auteurs ont mis au point une technique rapide d'e´lectrophore`se capillaire (EC) pour se´parer les prote´ines hydrosolubles en recourant a`des colonnes de silice fondue et a`une solution de phosphate acide tamponne´e a`la glycine. Pour la meilleure re´solution et la reproductibilite´optimale de la se´paration par EC, ils ont examine´diverses me´thodes d'extraction des prote´ines, plusieurs modificateurs organiques du tampon phosphate-glycine et diffe´rents parame`tres de l'e´lectrophore`se capillaire, parmi lesquels la longueur et le diame`tre inte´rieur (DI) des capillaires, la tempe´rature et la tension durant l'ope´ration et la d...

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Proteomic analysis of the effect of heat stress on hexaploid wheat grain: Characterization of heat‐responsive proteins from non‐prolamins fraction

Cited by 188 publications

References 43 publications

A proteomic approach in analyzing heat‐responsive proteins in rice leaves

A proteomic approach in analyzing heat‐responsive proteins in rice leaves

Systems-Wide Analysis of Acclimation Responses to Long-Term Heat Stress and Recovery in the Photosynthetic Model OrganismChlamydomonas reinhardtii

Rapid separation and characterization of grain water-soluble proteins in bread wheat cultivars (Triticum aestivum L.) by capillary electrophoresis

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