A novel LEA gene from Tamarix androssowii confers drought tolerance in transgenic tobacco

Wang, Yucheng; Jiang, Jing; Zhao, Xin; Liu, Guifeng; Yang, Chuanping; Zhan, Linlin

doi:10.1016/j.plantsci.2006.06.011

Cited by 68 publications

(52 citation statements)

References 25 publications

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“…The hydrophilic characteristic of LEA proteins may help protect specific cellular structures or ameliorate the effect of dryness during embryogenesis through attracting water or other polar molecules. Likewise, Wang et al (2006) have reported that LEA proteins are the members of a large group of hydrophilic proteins. Their mechanism of function could be fulfilled through: Maintaining protein or membrane structure, sequestration of ions, binding of water, or operation as molecular chaperones to help prevent the formation of damaging protein aggregates.…”

Section: Discussionmentioning

confidence: 98%

A Proteomics Analysis of Drought Stress-Responsive Proteins as Biomarker for Drought-Tolerant Sugarcane Cultivars

Jangpromma¹,

Kitthaisong²,

Lomthaisong³

et al. 2010

American Journal of Biochemistry and Biotechnology

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Problem statement:The prime objective in breeding selection process of drought-tolerant sugarcane is to identify the correlating marker, which could lead to rapid screening for drought-tolerant cultivars. In this study, we have reported an unknown 18-kDa protein (p18) along with other stress-inducible proteins to be highly expressed in sugarcane leaves under drought stress condition. Approach: The 2D-PAGE patterns of proteins were compared between those expressed in drought-tolerance K86-161 and drought-susceptible Khon Kaen 1 cultivars. The interested proteins were identified by mass spectrometry. The correlation between p18 expression and drought tolerance was verified in additional 4 sugarcane cultivars using ELISA and western blotting. Two physiological indexes, Chlorophyll content and SOD activity were also evaluated. Results: Mass spectrometry and comparison with known sequences in the database reveal that the proteins expressed only in stressed K86-161 are serine protease inhibitor and the one similar to replication protein A1. A group of proteins up-regulated in K86-161 are SAdenosylmethionine decarboxylase proenzyme (SAM), ubiquitin and p18. From ELISA and western blotting analysis, we found that p18 expressed in drought-tolerant sugarcane cultivars had higher binding specificity to antibody than that in drought-susceptible sugarcane cultivars. Two physiological indexes showed higher levels in drought-tolerant than those in drought susceptible sugarcanes. Conclusion: These high levels of chlorophyll and SOD are in agreement with a high level of p18 expression in droughttolerant sugarcanes. It is likely that an accumulation of p18 is a response to water deficit. In conclusion, p18 might be a good candidate for development as a marker in drought-tolerant plants.

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Section: Discussionmentioning

confidence: 98%

A Proteomics Analysis of Drought Stress-Responsive Proteins as Biomarker for Drought-Tolerant Sugarcane Cultivars

Jangpromma¹,

Kitthaisong²,

Lomthaisong³

et al. 2010

American Journal of Biochemistry and Biotechnology

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“…This gene was recently identified in a screen for genes involved in oxidative stress tolerance and has been suggested to play a role in the controlled degradation of the photosynthetic apparatus in the dark and under stress conditions (64 -66). Another study showed that transgenic Nicotiana tabacum overexpressing a Lea5 member from the shrub Tamarix androssowii had increased tolerance against desiccation and clear indications of reduced oxidative stress (67). Interestingly, two Lea5 members from poplar were recently shown to be upregulated in rust (fungus)-infected leaves, which are known to elicit the ROS-associated hypersensitive plant defense response (68).…”

Section: Discussionmentioning

confidence: 99%

An Unusual Intrinsically Disordered Protein from the Model Legume Lotus japonicus Stabilizes Proteins in Vitro

Haaning

Radutoiu

Hoffmann³

et al. 2008

Journal of Biological Chemistry

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Intrinsic structural disorder is a prevalent feature of proteins with chaperone activity. Using a complementary set of techniques, we have structurally characterized LjIDP1 (intrinsically disordered protein 1) from the model legume Lotus japonicus, and our results provide the first structural characterization of a member of the Lea5 protein family (PF03242). Contrary to in silico predictions, we show that LjIDP1 is intrinsically disordered and probably exists as an ensemble of conformations with limited residual ␤-sheet, turn/loop, and polyproline II secondary structure. Furthermore, we show that LjIDP1 has an inherent propensity to undergo a large conformational shift, adopting a largely ␣-helical structure when it is dehydrated and in the presence of different detergents and alcohols. This is consistent with an overrepresentation of order-promoting residues in LjIDP1 compared with the average of intrinsically disordered proteins. In line with functioning as a chaperone, we show that LjIDP1 effectively prevents inactivation of two model enzymes under conditions that promote protein misfolding and aggregation. The LjIdp1 gene is expressed in all L. japonicus tissues tested. A higher expression level was found in the root tip proximal zone, in roots inoculated with compatible endosymbiotic M. loti, and in functional nitrogen-fixing root nodules. We suggest that the ability of LjIDP1 to prevent protein misfolding and aggregation may play a significant role in tissues, such as symbiotic root nodules, which are characterized by high metabolic activity.Intrinsically disordered (or natively unfolded) proteins (IDPs) 5 that are disordered along the entire amino acid chain or contain long disordered regions have recently attracted attention due to their role in important human diseases and their distinct functional features (1). In plants, a loosely defined group of stress-related proteins known as the late embryogenesis-abundant (LEA) proteins are characterized by being almost exclusively intrinsically disordered (reviewed by Tunnacliffe and Wise (2)). Several lines of evidence suggest a role of LEA proteins in the protection against damage caused by different types of stress, in particular desiccation, salt, and cold stress. The exact protection mechanism is unknown; however, the demonstrated ability of some (and probably most) LEA proteins to adopt a more well ordered conformation upon the addition of structure perturbing chemicals and when dried may contribute (2). Such structural plasticity is also known from other IDPs, which undergo disorder-to-order transitions upon ligand binding (3). However, specific ligand interactions have not been described for any LEA protein, and the mechanism by which LEA proteins assert their functions remains elusive.We report here the biochemical characterization of the LjIDP1 protein encoded by the LjIdp1 gene that is up-regulated during nodule development and in functional nitrogen-fixing nodules of the model legume Lotus japonicus. Leguminous plants are unique in their ability to ...

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“…Previous studies have demonstrated that overexpression of LEA proteins in transgenic rice, wheat, tobacco, and Chinese cabbage enhances their resistance to drought and salt stresses (Xu et al, 1996;Sivamani et al, 2000;Park et al, 2005;Wang et al, 2006). Moreover, the LE25 protein or hiC6 protein, expressed in yeast, confers improved resistance to high salinity and freezing (Imai et al, 1996;Honjoh et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…Although LEA genes have been isolated and studied in many plants (Moons et al, 1997;Shih et al, 2004;Wang et al, 2006), no examinations have been made in its cloning, molecular characterization, or expression in any alpine subnival plant. It remains unclear whether expression of the C. bungeana LEA gene changes in response to abiotic stresses, and the functioning of the C. bungeana LEA protein in stress tolerance is another important, unsolved problem.…”

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confidence: 99%

CbLEA, a NovelLEA Gene fromChorispora bungeana, Confers Cold Tolerance in Transgenic Tobacco

et al. 2007

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A novel late embryogenesis abundant (LEA) gene (AY804193), named CbLEA, has now been isolated from Chorispora bungeana. This rare alpine subnival plant can survive sudden snowstorms and low temperatures. The full-length CbLEA is 842 bp, with an open reading frame encoding 169 amino acids. The putative molecular weight of CbLEA protein is 17.9 kDa, with an estimated pl of 6.45. To investigate the functioning of this CbLEA protein in cold-stress tolerance, CbLEA was introduced into tobacco under the control of the CaMV35S promoter. Second-generation (R1) transgenic tobacco plants exhibited significantly increased tolerance to cold. These transgenics maintained lower malondialdehyde (MDA) contents and electrolyte leakage (EL) but their relative water content (RWC) was significantly higher compared with non-transgenic plants under chilling stress. Further experimental results showed that non-transgenic plants had severe freezing damage after exposure to -2~ for 1 h, whereas the transgenics suffered only slight injury under the same conditions. Moreover, survival was longer in the latter genotype at that temperature. The extent of increased cold tolerance was positive correlated with the level of CbLEA protein accumulation, and was also reflected by the delayed development of damage symptoms. This indicates that CbLEA is an excellent stress tolerance gene, and holds considerable potential as a new molecular tool for engineering improved plant genetics.

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A novel LEA gene from Tamarix androssowii confers drought tolerance in transgenic tobacco

Cited by 68 publications

References 25 publications

A Proteomics Analysis of Drought Stress-Responsive Proteins as Biomarker for Drought-Tolerant Sugarcane Cultivars

A Proteomics Analysis of Drought Stress-Responsive Proteins as Biomarker for Drought-Tolerant Sugarcane Cultivars

An Unusual Intrinsically Disordered Protein from the Model Legume Lotus japonicus Stabilizes Proteins in Vitro

CbLEA, a NovelLEA Gene fromChorispora bungeana, Confers Cold Tolerance in Transgenic Tobacco

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