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Tao Wang - One of the best experts on this subject based on the ideXlab platform.
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mtcas31 aids symbiotic nitrogen fixation by protecting the leghemoglobin mtlb120 1 under drought stress in medicago truncatula
Frontiers in Plant Science, 2018Co-Authors: Hao Feng, Jiangqi Wen, Jiangli Dong, Tao WangAbstract:Symbiotic nitrogen fixation (SNF) in legume root nodules injects millions of tons of nitrogen into agricultural lands and provides ammonia to non-legume crops under N-deficient conditions. During plant growth and development, environmental stresses, such as drought, salt, cold, and heat stress are unavoidable. This raises an interesting question as to how the legumes cope with the environmental stress along with SNF. Under drought stress, dehydrin proteins are accumulated, which function as protein protector and osmotic substances. In this study, we found that the dehydrin MtCAS31 (cold-acclimation-specific 31) functions in SNF in Medicago truncatula during drought stress. We found that MtCAS31 is expressed in nodules and interacts with leghemoglobin MtLb120-1. The interaction between the two proteins protects MtLb120-1 from denaturation under thermal stress in vivo. Compared to wild type, cas31 mutants display a lower nitrogenase activity, a lower ATP/ADP ratio, higher expression of nodule senescence genes and higher accumulation of amyloplasts under dehydration conditions. The results suggested that MtCAS31 protects MtLb120-1 from the damage of drought stress. We identified a new function for Dehydrins in SNF under drought stress, which enriches the understanding of the molecular mechanism of Dehydrins.
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Image_3_MtCAS31 Aids Symbiotic Nitrogen Fixation by Protecting the Leghemoglobin MtLb120-1 Under Drought Stress in Medicago truncatula.TIF
2018Co-Authors: Hao Feng, Jiangqi Wen, Jiangli Dong, Tao WangAbstract:Symbiotic nitrogen fixation (SNF) in legume root nodules injects millions of tons of nitrogen into agricultural lands and provides ammonia to non-legume crops under N-deficient conditions. During plant growth and development, environmental stresses, such as drought, salt, cold, and heat stress are unavoidable. This raises an interesting question as to how the legumes cope with the environmental stress along with SNF. Under drought stress, dehydrin proteins are accumulated, which function as protein protector and osmotic substances. In this study, we found that the dehydrin MtCAS31 (cold-acclimation-specific 31) functions in SNF in Medicago truncatula during drought stress. We found that MtCAS31 is expressed in nodules and interacts with leghemoglobin MtLb120-1. The interaction between the two proteins protects MtLb120-1 from denaturation under thermal stress in vivo. Compared to wild type, cas31 mutants display a lower nitrogenase activity, a lower ATP/ADP ratio, higher expression of nodule senescence genes and higher accumulation of amyloplasts under dehydration conditions. The results suggested that MtCAS31 protects MtLb120-1 from the damage of drought stress. We identified a new function for Dehydrins in SNF under drought stress, which enriches the understanding of the molecular mechanism of Dehydrins.
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Table_1_MtCAS31 Aids Symbiotic Nitrogen Fixation by Protecting the Leghemoglobin MtLb120-1 Under Drought Stress in Medicago truncatula.DOCX
2018Co-Authors: Hao Feng, Jiangqi Wen, Jiangli Dong, Tao WangAbstract:Symbiotic nitrogen fixation (SNF) in legume root nodules injects millions of tons of nitrogen into agricultural lands and provides ammonia to non-legume crops under N-deficient conditions. During plant growth and development, environmental stresses, such as drought, salt, cold, and heat stress are unavoidable. This raises an interesting question as to how the legumes cope with the environmental stress along with SNF. Under drought stress, dehydrin proteins are accumulated, which function as protein protector and osmotic substances. In this study, we found that the dehydrin MtCAS31 (cold-acclimation-specific 31) functions in SNF in Medicago truncatula during drought stress. We found that MtCAS31 is expressed in nodules and interacts with leghemoglobin MtLb120-1. The interaction between the two proteins protects MtLb120-1 from denaturation under thermal stress in vivo. Compared to wild type, cas31 mutants display a lower nitrogenase activity, a lower ATP/ADP ratio, higher expression of nodule senescence genes and higher accumulation of amyloplasts under dehydration conditions. The results suggested that MtCAS31 protects MtLb120-1 from the damage of drought stress. We identified a new function for Dehydrins in SNF under drought stress, which enriches the understanding of the molecular mechanism of Dehydrins.
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Data_Sheet_2_MtCAS31 Aids Symbiotic Nitrogen Fixation by Protecting the Leghemoglobin MtLb120-1 Under Drought Stress in Medicago truncatula.XLSX
2018Co-Authors: Hao Feng, Jiangqi Wen, Jiangli Dong, Tao WangAbstract:Symbiotic nitrogen fixation (SNF) in legume root nodules injects millions of tons of nitrogen into agricultural lands and provides ammonia to non-legume crops under N-deficient conditions. During plant growth and development, environmental stresses, such as drought, salt, cold, and heat stress are unavoidable. This raises an interesting question as to how the legumes cope with the environmental stress along with SNF. Under drought stress, dehydrin proteins are accumulated, which function as protein protector and osmotic substances. In this study, we found that the dehydrin MtCAS31 (cold-acclimation-specific 31) functions in SNF in Medicago truncatula during drought stress. We found that MtCAS31 is expressed in nodules and interacts with leghemoglobin MtLb120-1. The interaction between the two proteins protects MtLb120-1 from denaturation under thermal stress in vivo. Compared to wild type, cas31 mutants display a lower nitrogenase activity, a lower ATP/ADP ratio, higher expression of nodule senescence genes and higher accumulation of amyloplasts under dehydration conditions. The results suggested that MtCAS31 protects MtLb120-1 from the damage of drought stress. We identified a new function for Dehydrins in SNF under drought stress, which enriches the understanding of the molecular mechanism of Dehydrins.
Rajeev Arora - One of the best experts on this subject based on the ideXlab platform.
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Identification and Characterization of Five Cold Stress-Related Rhododendron Dehydrin Genes: Spotlight on a FSK-Type Dehydrin With Multiple F-Segments.
Frontiers in bioengineering and biotechnology, 2019Co-Authors: Hui Wei, Yongfu Yang, Michael E. Himmel, Melvin P. Tucker, Shi-you Ding, Shihui Yang, Rajeev AroraAbstract:Dehydrins are a family of plant proteins that accumulate in response to dehydration stresses, such as low temperature, drought, high salinity, or during seed maturation. We have previously constructed cDNA libraries from Rhododendron catawbiense leaves of naturally non-acclimated (NA; leaf LT50, temperature that results in 50% injury of maximum, approximately -7 oC) and cold-acclimated (CA; leaf LT50 approximately -50 oC) plants and analyzed expressed sequence tags (ESTs). Five ESTs were identified as dehydrin genes. Their full-length cDNA sequences were obtained and designated as RcDhn 1-5. To explore their functionality vis-a-vis winter hardiness, their seasonal expression kinetics was studied at two levels. Firstly, in leaves of R. catawbiense collected from the NA, CA, and de-acclimated (DA) plants corresponding to summer, winter and spring, respectively. Secondly, in leaves collected monthly from August through February, which progressively increased freezing tolerance from summer through mid-winter. The expression pattern data indicated that RcDhn 1-5 had 6- to 15-fold up-regulation during the cold acclimation process, followed by substantial down-regulation during deacclimation (even back to NA levels for some). Interestingly, our data shows RcDhn 5 contains a histidine-rich motif near N-terminus, a characteristic of metal-binding Dehydrins. Equally important, RcDhn 2 contains a consensus 18 amino acid sequence (i.e., ETKDRGLFDFLGKKEEEE) near the N-terminus, with two additional copies upstream, and it is the most acidic (pI of 4.8) among the five RcDhns found. The core of this consensus 18 amino acid sequence is a 11-residue amino acid sequence (DRGLFDFLGKK), recently designated in the literature as the F segment (based on the pair of hydrophobic F residues it contains). Furthermore, the 208 orthologs of F-segment-containing RcDhn 2 were identified across a broad range of species in GenBank database. This study expands our knowledge about the types of F-segment from the literature-reported single F-segment Dehydrins (FSKn) to two or three F-segment Dehydrins: Camelina sativa dehydrin ERD14 as F2S2Kn type; and RcDhn 2 as F3SKn type identified here. Our results also indicate some consensus amino acid sequences flanking the core F-segment in Dehydrins. Implications for these cold-responsive RcDhn genes in future genetic engineering efforts to improve plant cold hardiness are discussed.
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Table_2_Identification and Characterization of Five Cold Stress-Related Rhododendron Dehydrin Genes: Spotlight on a FSK-Type Dehydrin With Multiple F-Segments.XLSX
2019Co-Authors: Hui Wei, Yongfu Yang, Michael E. Himmel, Melvin P. Tucker, Shi-you Ding, Shihui Yang, Rajeev AroraAbstract:Dehydrins are a family of plant proteins that accumulate in response to dehydration stresses, such as low temperature, drought, high salinity, or during seed maturation. We have previously constructed cDNA libraries from Rhododendron catawbiense leaves of naturally non-acclimated (NA; leaf LT50, temperature that results in 50% injury of maximum, approximately −7°C) and cold-acclimated (CA; leaf LT50 approximately −50°C) plants and analyzed expressed sequence tags (ESTs). Five ESTs were identified as dehydrin genes. Their full-length cDNA sequences were obtained and designated as RcDhn 1-5. To explore their functionality vis-à-vis winter hardiness, their seasonal expression kinetics was studied at two levels. Firstly, in leaves of R. catawbiense collected from the NA, CA, and de-acclimated (DA) plants corresponding to summer, winter and spring, respectively. Secondly, in leaves collected monthly from August through February, which progressively increased freezing tolerance from summer through mid-winter. The expression pattern data indicated that RcDhn 1-5 had 6- to 15-fold up-regulation during the cold acclimation process, followed by substantial down-regulation during deacclimation (even back to NA levels for some). Interestingly, our data shows RcDhn 5 contains a histidine-rich motif near N-terminus, a characteristic of metal-binding Dehydrins. Equally important, RcDhn 2 contains a consensus 18 amino acid sequence (i.e., ETKDRGLFDFLGKKEEEE) near the N-terminus, with two additional copies upstream, and it is the most acidic (pI of 4.8) among the five RcDhns found. The core of this consensus 18 amino acid sequence is a 11-residue amino acid sequence (DRGLFDFLGKK), recently designated in the literature as the F-segment (based on the pair of hydrophobic F residues it contains). Furthermore, the 208 orthologs of F-segment-containing RcDhn 2 were identified across a broad range of species in GenBank database. This study expands our knowledge about the types of F-segment from the literature-reported single F-segment Dehydrins (FSKn) to two or three F-segment Dehydrins: Camelina sativa dehydrin ERD14 as F2S2Kn type; and RcDhn 2 as F3SKn type identified here. Our results also indicate some consensus amino acid sequences flanking the core F-segment in Dehydrins. Implications for these cold-responsive RcDhn genes in future genetic engineering efforts to improve plant cold hardiness are discussed.
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Isolation and characterization of three cold acclimation-responsive dehydrin genes from Eucalyptus globulus
Tree Genetics & Genomes, 2012Co-Authors: Marta Fernandez, Rajeev Arora, Sofia Valenzuela Águila, Keting ChenAbstract:The molecular and physiological work related to cold hardiness in Eucalyptus globulus and the cold-responsive Dehydrins is reported. The identification and full-length gene sequence of three Dehydrins of 10, 20, and 30 kDa and the comparison of their promoters regarding to potential stress and hormone response elements in E. globulus are shown. The categorization of cold-responsive proteins as dehydrin was based on the similarity in amino acid composition with selected sequenced peptides from chilling-responsive dehydrin reported for other woody plants and the increasing of gene expression level during cold acclimation. The transcript accumulation for these three dehydrin genes increased with cold acclimation and decreased with deacclimation in leaf and stem tissues, being higher in a freezing-resistant genotype of E. globulus compared to a sensitive genotype. By western blot, five dehydrin peptides were identified which increased their expression, under cold stress in leaf and stem tissues. These results provide valuable information about cold acclimation and gene regulation in eucalypt genotypes that differ in their ability to tolerate frost temperature.
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Dehydrin variability among rhododendron species: a 25-kDa dehydrin is conserved and associated with cold acclimation across diverse species
New Phytologist, 2004Co-Authors: Calin O. Marian, Stephen L. Krebs, Rajeev AroraAbstract:Summary • Here we examine the accumulation pattern of Dehydrins in non- vs cold-acclimated leaves of 21 species comprising two divergent groups of Rhododendron, Subgenus Hymenanthes and Subgenus Rhododendron. Individuals from five other Ericaceous genera were also evaluated in the same way. Quantitative comparisons of cold-inducibility of a 25-kDa dehydrin and cold acclimation ability in six Rhododendron species were also performed. • Leaf freezing tolerance assay and dehydrin detection and quantification were performed as previously described. • Eleven Dehydrins, ranging from 25- to 73-kDa, were observed among the 21 species, and most were more abundant in winter-collected leaves than in summer-collected leaves. One dehydrin, a 25-kDa protein, was uniquely conserved across most (95%) of the species surveyed, and was absent only in R. brookeanum, a tropical species that may not be capable of cold acclimation. The 25-kDa dehydrin was also identified in Kalmia, a genus closely related to Rhododendron but not in four other less related Ericaceous genera. Comparison of dehydrin profiles in non- and cold-acclimated leaf tissue from six species (three very hardy, and three less hardy, species) indicated a close association (R2 = 0.95) between relative changes in leaf freezing tolerance and 25-kDa dehydrin accumulation. • The taxonomic and physiological comparisons suggest a central, but as yet unknown, function for the 25-kDa dehydrin in protecting rhododendron leaves from freezing injury.
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Complementary DNA cloning, sequencing and expression of an unusual dehydrin from blueberry floral buds
Physiologia Plantarum, 1999Co-Authors: Amnon Levi, Rajeev Arora, Ganesh R. Panta, Cécile M. Parmentier, Mubarack M. Muthalif, Savita Shanker, Lisa J. RowlandAbstract:Levels of three major Dehydrins of 65, 60, and 14 kDa have been observed to increase in blueberry (Vaccinium spp.) floral buds during chill unit accumulation and cold acclimation and decrease during deacclimation and resumption of growth. Indeed, levels of the 65-, 60-, and 14-kDa Dehydrins increase such that they become the most predominant proteins visible on sodium dodecyl sulfate (SDS)-polyacrylamide gels. The peptide sequence information from the 65- and 60-kDa Dehydrins was used to synthesize degenerate DNA primers for amplification of a part of the gene(s) encoding the Dehydrins. One pair of primers amplified a 174-bp fragment. The 174-bp fragment was used to screen a cDNA library (prepared from RNA from cold-acclimated blueberry floral buds) and resulted in the isolation of a clone with a 2.0-kb insert. The cDNA was sequenced and found to be a full-length clone encoding a K 5 -type dehydrin (5 K boxes). Five high-confidence peptide sequences, ranging from 9 to 25 amino acids long, obtained from the 60-kDa dehydrin exactly matched sequences encoded within the cDNA clone. Furthermore, amino acid composition of the 60-kDa dehydrin agreed well with the expected amino acid composition based on the cDNA sequence. However, the DNA sequence and coupled in vitro transcription/translation reactions of the cDNA clone indicated that it encodes a dehydrin with a native molecular mass of ∼ 40 kDa instead of 60 kDa. Experiments to determine if the Dehydrins undergo post-translational modifications revealed that the 65- and 60-kDa Dehydrins are glycosylated. Thus, our results indicate that the 2.0-kb dehydrin cDNA encodes the native version of the 60-kDa dehydrin. The dehydrin cDNA hybridized on RNA blots to two chilling/cold-responsive messages of 2.0 and 0.5 kb. Both the 2.0- and 0.5-kb messages increased to higher levels more quickly in the cold-hardy cultivar Bluecrop than in the less hardy cultivar Tifblue. In addition, the 0.5-kb message remained at a higher level longer in Bluecrop than in Tifblue.
Timothy J. Close - One of the best experts on this subject based on the ideXlab platform.
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purification immunolocalization cryoprotective and antifreeze activity of pca60 a dehydrin from peach prunus persica
Physiologia Plantarum, 1999Co-Authors: Michael Wisniewski, Timothy J. Close, Ron Balsamo, Robert Webb, Marilyn GriffithAbstract:Dehydrins are glycine-rich, hydrophilic, heat-stable proteins and are generally induced in response to a wide array of environmental stresses. In previous research (Artlip et al. 1997, Plant Molecular Biology 33: 61-70), a full-length dehydrin gene, ppdhn1, was isolated from peach, and its expression was associated with qualitative and quantitative differences in cold hardiness in sibling genotypes of evergreen and deciduous peach. Similar results were obtained for levels of the corresponding 60 kDa peach dehydrin protein (PCA60). The objective of the present study was to purify the PCA60, test the purified protein for cryoprotective and/or antifreeze activity, and to determine the cellular localization of PCA60 using immunomicroscopy. PCA60 was extracted from winter bark tissues of peach (Prunus persica [L.] Batsch) and purified in a two-step process. Separation was based on free-solution isoelectric focusing followed by size exclusion. Purified PCA60, as well as crude protein extract, preserved the in vitro enzymatic activity of lactate dehydrogenase after several freeze-thaw cycles in liquid nitrogen. PCA also exhibited distinct antifreeze activity as evidenced by ice crystal morphology and thermal hysteresis. This is the first time antifreeze activity has been demonstrated for Dehydrins. Immunomicroscopy, utilizing an affinity-purified, polyclonal antibody developed against a synthetic peptide of the lysine-rich consensus portion of Dehydrins, indicated that PCA60 was freely distributed in the cytoplasm, plastids, and nucleus of bark cells and xylem parenchyma cells. Although the functional role of Dehydrins remains speculative, the data support the hypothesis that it plays a role in preventing denaturation of proteins exposed to dehvdrative stresses.
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genetic studies of triticeae Dehydrins assignment of seed proteins and a regulatory factor to map positions
Theoretical and Applied Genetics, 1998Co-Authors: J E Wernerfraczek, Timothy J. CloseAbstract:A collection of 200 wheat (Triticum aestivum L. cv ‘Chinese Spring’) cytogenetic stocks (nullisomic, tetrasomic, nulli-tetrasomic, ditelosomic and deletion lines, addition and substitution stocks from intra- and inter-specific crosses) was utilized to determine the proteins encoded by some of the wheat and barley dehydrin genes, using a western blot procedure. Proteins extracted from seeds were reacted with antibodies that recognize Dehydrins in a wide range of plants, including wheat and barley. Proteins encoded by dehydrin loci in chromosome arms 4DS, 5BL and 6AL of ‘Chinese Spring’ wheat were assigned by this method. There was also evidence of a regulatory factor on 5B in the vicinity of the dhn genes, and on 5H in wheat-barley addition lines, that is required for a normal level of expression of seed Dehydrins in hexaploid wheat. Further understanding of this putative regulatory factor would be helpful for the interpretation of linkage studies that may relate dehydrin gene expression to phenotypes such as dehydration, salinity or low-temperature tolerance.
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Dehydrins a commonalty in the response of plants to dehydration and low temperature
Physiologia Plantarum, 1997Co-Authors: Timothy J. CloseAbstract:Among proteins that accumulate in plants in response to dehydrative forces or low temperature, Dehydrins (late embryogenesis abundant [Lea] D11 family) have been the most commonly observed. Dehydrins are composed of several typical domains joined together in a few characteristic patterns, with numerous minor permutations. These domains include one or more putative amphipathic a-helix forming consensus regions, a phosphorylatable tract of Ser residues, and an N-terminal consensus sequence. Lesser conserved domains are also present at various positions, particularly between the putative a-helix forming domains, where they may occur as tandem repeats. This medley of permutations is mirrored by a wide size range of dehydrin polypeptides from less than 100 to nearly 600 amino acid residues. As of yet, the fundamental biochemical mode of action of Dehydrins has not been demonstrated, but a number of immunolocalization and cell fractionation studies have established that Dehydrins can be located in the nucleus or cytoplasm. Furthermore, it appears that these proteins associate with macromolecules ranging from nucleoprotein complexes in the nucleus to an endomembrane sheath in the cytoplasm. At present, all observations are consistent with a hypothesis that Dehydrins are surfactants capable of inhibiting the coagulation of a range of macromolecules, thereby preserving structural integrity.
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Dehydrins: genes, proteins, and associations with phenotypic traits
New Phytologist, 1997Co-Authors: Scott A. Campbell, Timothy J. CloseAbstract:Dehydrin proteins (late embryogenesis abundant (LEA) D11 family) are produced in a wide variety of plant species in response to environmental stimuli with a dehydrative component, including drought, low temperature, salinity, and developmental stages such as seed and pollen maturation. Despite their widespread occurrence and abundance in cells under dehydrative conditions, the biochemical role of Dehydrins remains elusive. The subcellular location of Dehydrins is consistent with a biochemical role as an intracellular stabilizer, possibly with surfactant characteristics, acting upon targets in both the nucleus and cytoplasm. In some species, dehydrin loci are located within quantitative trait loci (QTL) intervals for important phenotypic traits including winter hardiness in barley (Hordeum vulgare L.) and anthesis-silking interval in maize (Zea mays L.). Dehydrin loci tend to be multigenic and occur in clusters on more than one chromosome. Investigations are currently under way in our laboratory and others' to move beyond protein accumulation studies and correlations with QTL to uncover direct cause-and-effect relationships between dehydrin (dhn) genes and phenotypes associated with physiological responses to stress.
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Temporal accumulation and ultrastructural localization of Dehydrins in Zea mays
Physiologia Plantarum, 1997Co-Authors: Louise M. Egerton-warburton, Ronald A. Balsamo, Timothy J. CloseAbstract:Immunolocalization using polyclonal antibodies raised against a conserved dehydrin amino acid sequence was used to establish the temporal and spatial patterns of dehydrin accumulation in embryo tissue of Zea mays L. (var. Ohio 43) kernels imbibed in the presence of abscisic acid. The temporal pattern of accumulation indicated an increase in Dehydrins over time (particularly between 15 and 30 h) and with maximum levels detected 48 h after the onset of imbibition. Dehydrins were first evident, and also the most concentrated, in the cytosol throughout the accumulation period suggesting that the primary function of Dehydrins involves the cytosol and the structures contained therein. Only after an accumulation of Dehydrins in the cytosol was there an increase in the abundance of nuclear Dehydrins. In addition, Dehydrins were also observed in association with the proteinaceous matrix of protein bodies and membranes of protein and lipid bodies; these findings have not been reported previously. The observed localization at a number of sites indicates that the specific biochemical roles of Dehydrins are likely to be diverse.
Ilja Tom Prášil - One of the best experts on this subject based on the ideXlab platform.
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Relationship Between Dehydrin Accumulation and Winter Survival in Winter Wheat and Barley Grown in the Field
Frontiers Media S.A., 2019Co-Authors: Pavel Vítámvás, Klára Kosová, Jana Musilová, Ludmila Holková, Pavel Mařík, Pavlína Smutná, Miroslav Klíma, Ilja Tom PrášilAbstract:Low temperatures represent a crucial environmental factor determining winter survival (WS) of barley and wheat winter-type varieties. In laboratory experiments, low temperatures induce an active plant acclimation response, which is associated with an enhanced accumulation of several stress-inducible proteins including Dehydrins. Here, dehydrin accumulations in sampled wheat (WCS120 protein family, or WCS120 and WDHN13 transcripts) and barley (DHN5 protein) varieties grown in two locations for two winters were compared with the variety WS evaluated by a provocation wooden-box test. A high correlation between dehydrin transcripts or protein relative accumulation and variety WS score was found only in samples taken prior vernalization fulfillment, when high tolerant varieties accumulated Dehydrins earlier and to higher level than less tolerant varieties, and the plants have not yet been vernalized. After vernalization fulfillment, the correlation was weak, and the apical development indicated that plants reached double ridge (DR) in barley or stayed before DR in wheat. Dehydrin proteins and transcripts can be thus used as reliable markers of wheat or barley variety winter hardiness in the field conditions; however, only at the beginning of winter, when the plants have not yet finished vernalization. In wheat, a higher correlation was obtained for the total amount of Dehydrins than for the individual dehydrin proteins.HIGHLIGHTS-More tolerant winter-type wheat and barley plants reveal higher threshold induction temperatures for dehydrin accumulation in comparison to less tolerant varieties. Thus, more tolerant winter cereals have higher dehydrin levels than the less tolerant ones upon the same ambient temperature in November samplings.-A significant correlation between dehydrin transcript/protein accumulation and winter survival was found in both winter wheat and winter barley plants in the field conditions, but only prior to vernalization fulfillment
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Data_Sheet_1_Relationship Between Dehydrin Accumulation and Winter Survival in Winter Wheat and Barley Grown in the Field.docx
2019Co-Authors: Pavel Vítámvás, Klára Kosová, Jana Musilová, Ludmila Holková, Pavel Mařík, Pavlína Smutná, Miroslav Klíma, Ilja Tom PrášilAbstract:Low temperatures represent a crucial environmental factor determining winter survival (WS) of barley and wheat winter-type varieties. In laboratory experiments, low temperatures induce an active plant acclimation response, which is associated with an enhanced accumulation of several stress-inducible proteins including Dehydrins. Here, dehydrin accumulations in sampled wheat (WCS120 protein family, or WCS120 and WDHN13 transcripts) and barley (DHN5 protein) varieties grown in two locations for two winters were compared with the variety WS evaluated by a provocation wooden-box test. A high correlation between dehydrin transcripts or protein relative accumulation and variety WS score was found only in samples taken prior vernalization fulfillment, when high tolerant varieties accumulated Dehydrins earlier and to higher level than less tolerant varieties, and the plants have not yet been vernalized. After vernalization fulfillment, the correlation was weak, and the apical development indicated that plants reached double ridge (DR) in barley or stayed before DR in wheat. Dehydrin proteins and transcripts can be thus used as reliable markers of wheat or barley variety winter hardiness in the field conditions; however, only at the beginning of winter, when the plants have not yet finished vernalization. In wheat, a higher correlation was obtained for the total amount of Dehydrins than for the individual dehydrin proteins.HIGHLIGHTS-More tolerant winter-type wheat and barley plants reveal higher threshold induction temperatures for dehydrin accumulation in comparison to less tolerant varieties. Thus, more tolerant winter cereals have higher dehydrin levels than the less tolerant ones upon the same ambient temperature in November samplings.-A significant correlation between dehydrin transcript/protein accumulation and winter survival was found in both winter wheat and winter barley plants in the field conditions, but only prior to vernalization fulfillment.
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wheat and barley Dehydrins under cold drought and salinity what can lea ii proteins tell us about plant stress response
Frontiers in Plant Science, 2014Co-Authors: Klára Kosová, Pavel Vítámvás, Ilja Tom PrášilAbstract:Dehydrins as a group of Late embryogenesis abundant II (LEA-II) proteins represent important dehydration-inducible proteins whose accumulation is induced by developmental processes (embryo maturation) as well as by several abiotic stress factors (low temperatures, drought, salinity). In the review, an overview of studies aimed at investigation of dehydrin accumulation patterns at transcript and protein levels as well as their possible functions in common wheat (Triticum aestivum), durum wheat (Triticum durum) and barley (Hordeum vulgare) plants exposed to various abiotic stress factors (cold, frost, drought, salinity) is provided. Possible roles of dehydrin proteins in an acquisition and maintenance of an enhanced frost tolerance are analysed in the context of plant developmental processes (vernalization). Quantitative and qualitative differences as well as posttranslational modifications in accumulated dehydrin proteins between barley cultivars revealing differential tolerance to drought and salinity are also discussed. Current knowledge on dehydrin role in wheat and barley response to major dehydrative stresses is summarized and the major challenges in dehydrin research are outlined.
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Expression of Dehydrins in wheat and barley under different temperatures
Plant science : an international journal of experimental plant biology, 2010Co-Authors: Klára Kosová, Pavel Vítámvás, Ilja Tom PrášilAbstract:The review summarizes recent knowledge on the expression of cold-inducible Dehydrins with a special attention to Wcs120 and Dhn5 genes in wheat and barley plants under different temperatures. When plants are exposed to cold, Dehydrins start accumulating both in freezing-tolerant and freezing-susceptible plants; however, their accumulation correlates with plant acquired frost tolerance (FT). During a long-term cold acclimation (CA), dehydrin accumulation is significantly affected by Vrn1/Fr1 locus and the expression of the major vernalization gene VRN1, respectively. A different dynamics of dehydrin transcripts and proteins during CA is also observed. Transcripts reach their maximum within the first week of CA while proteins gradually accumulate until vernalization. Vernalization is associated with a significant decrease in dehydrin accumulation while the decrease of acquired FT is delayed. Studies carried out on plants grown at moderately cold temperatures (9-20 °C) have shown that both dehydrin transcripts and proteins can be detected even at these temperatures and that plants with different FT levels can be distinguished according to dehydrin accumulation without any exposure to severe cold. In conclusion, the potential use of these results in the breeding programmes aimed at the enhancement of wheat and barley FT is discussed.
Hao Feng - One of the best experts on this subject based on the ideXlab platform.
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mtcas31 aids symbiotic nitrogen fixation by protecting the leghemoglobin mtlb120 1 under drought stress in medicago truncatula
Frontiers in Plant Science, 2018Co-Authors: Hao Feng, Jiangqi Wen, Jiangli Dong, Tao WangAbstract:Symbiotic nitrogen fixation (SNF) in legume root nodules injects millions of tons of nitrogen into agricultural lands and provides ammonia to non-legume crops under N-deficient conditions. During plant growth and development, environmental stresses, such as drought, salt, cold, and heat stress are unavoidable. This raises an interesting question as to how the legumes cope with the environmental stress along with SNF. Under drought stress, dehydrin proteins are accumulated, which function as protein protector and osmotic substances. In this study, we found that the dehydrin MtCAS31 (cold-acclimation-specific 31) functions in SNF in Medicago truncatula during drought stress. We found that MtCAS31 is expressed in nodules and interacts with leghemoglobin MtLb120-1. The interaction between the two proteins protects MtLb120-1 from denaturation under thermal stress in vivo. Compared to wild type, cas31 mutants display a lower nitrogenase activity, a lower ATP/ADP ratio, higher expression of nodule senescence genes and higher accumulation of amyloplasts under dehydration conditions. The results suggested that MtCAS31 protects MtLb120-1 from the damage of drought stress. We identified a new function for Dehydrins in SNF under drought stress, which enriches the understanding of the molecular mechanism of Dehydrins.
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Image_3_MtCAS31 Aids Symbiotic Nitrogen Fixation by Protecting the Leghemoglobin MtLb120-1 Under Drought Stress in Medicago truncatula.TIF
2018Co-Authors: Hao Feng, Jiangqi Wen, Jiangli Dong, Tao WangAbstract:Symbiotic nitrogen fixation (SNF) in legume root nodules injects millions of tons of nitrogen into agricultural lands and provides ammonia to non-legume crops under N-deficient conditions. During plant growth and development, environmental stresses, such as drought, salt, cold, and heat stress are unavoidable. This raises an interesting question as to how the legumes cope with the environmental stress along with SNF. Under drought stress, dehydrin proteins are accumulated, which function as protein protector and osmotic substances. In this study, we found that the dehydrin MtCAS31 (cold-acclimation-specific 31) functions in SNF in Medicago truncatula during drought stress. We found that MtCAS31 is expressed in nodules and interacts with leghemoglobin MtLb120-1. The interaction between the two proteins protects MtLb120-1 from denaturation under thermal stress in vivo. Compared to wild type, cas31 mutants display a lower nitrogenase activity, a lower ATP/ADP ratio, higher expression of nodule senescence genes and higher accumulation of amyloplasts under dehydration conditions. The results suggested that MtCAS31 protects MtLb120-1 from the damage of drought stress. We identified a new function for Dehydrins in SNF under drought stress, which enriches the understanding of the molecular mechanism of Dehydrins.
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Table_1_MtCAS31 Aids Symbiotic Nitrogen Fixation by Protecting the Leghemoglobin MtLb120-1 Under Drought Stress in Medicago truncatula.DOCX
2018Co-Authors: Hao Feng, Jiangqi Wen, Jiangli Dong, Tao WangAbstract:Symbiotic nitrogen fixation (SNF) in legume root nodules injects millions of tons of nitrogen into agricultural lands and provides ammonia to non-legume crops under N-deficient conditions. During plant growth and development, environmental stresses, such as drought, salt, cold, and heat stress are unavoidable. This raises an interesting question as to how the legumes cope with the environmental stress along with SNF. Under drought stress, dehydrin proteins are accumulated, which function as protein protector and osmotic substances. In this study, we found that the dehydrin MtCAS31 (cold-acclimation-specific 31) functions in SNF in Medicago truncatula during drought stress. We found that MtCAS31 is expressed in nodules and interacts with leghemoglobin MtLb120-1. The interaction between the two proteins protects MtLb120-1 from denaturation under thermal stress in vivo. Compared to wild type, cas31 mutants display a lower nitrogenase activity, a lower ATP/ADP ratio, higher expression of nodule senescence genes and higher accumulation of amyloplasts under dehydration conditions. The results suggested that MtCAS31 protects MtLb120-1 from the damage of drought stress. We identified a new function for Dehydrins in SNF under drought stress, which enriches the understanding of the molecular mechanism of Dehydrins.
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Data_Sheet_2_MtCAS31 Aids Symbiotic Nitrogen Fixation by Protecting the Leghemoglobin MtLb120-1 Under Drought Stress in Medicago truncatula.XLSX
2018Co-Authors: Hao Feng, Jiangqi Wen, Jiangli Dong, Tao WangAbstract:Symbiotic nitrogen fixation (SNF) in legume root nodules injects millions of tons of nitrogen into agricultural lands and provides ammonia to non-legume crops under N-deficient conditions. During plant growth and development, environmental stresses, such as drought, salt, cold, and heat stress are unavoidable. This raises an interesting question as to how the legumes cope with the environmental stress along with SNF. Under drought stress, dehydrin proteins are accumulated, which function as protein protector and osmotic substances. In this study, we found that the dehydrin MtCAS31 (cold-acclimation-specific 31) functions in SNF in Medicago truncatula during drought stress. We found that MtCAS31 is expressed in nodules and interacts with leghemoglobin MtLb120-1. The interaction between the two proteins protects MtLb120-1 from denaturation under thermal stress in vivo. Compared to wild type, cas31 mutants display a lower nitrogenase activity, a lower ATP/ADP ratio, higher expression of nodule senescence genes and higher accumulation of amyloplasts under dehydration conditions. The results suggested that MtCAS31 protects MtLb120-1 from the damage of drought stress. We identified a new function for Dehydrins in SNF under drought stress, which enriches the understanding of the molecular mechanism of Dehydrins.