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Aluminum Stress Induces Irreversible Proteomic Changes in the Roots of the Sensitive but Not the Tolerant Genotype of Triticale Seedlings.

Triticale is a wheat–rye hybrid with a higher abiotic stress tolerance than wheat and is better adapted for cultivation in light-type soils, where aluminum ions are present as Al-complexes that are harmful to plants. The roots are the first plant organs to contact these ions and the inhibition of root growth is one of the first plant reactions. The proteomes of the root apices in Al-tolerant and -sensitive plants were investigated to compare their regeneration effects following stress.

Niedziela, A., Domzalska, L., Dynkowska, W.M., Pernisová, M., Rybka, K. (2022)

Plants 2022, 11, 165. https://doi.org/10.3390/plants11020165

Abstract

Triticale is a wheat–rye hybrid with a higher abiotic stress tolerance than wheat and is better adapted for cultivation in light-type soils, where aluminum ions are present as Al-complexes that are harmful to plants. The roots are the first plant organs to contact these ions and the inhibition of root growth is one of the first plant reactions. The proteomes of the root apices in Al-tolerant and -sensitive plants were investigated to compare their regeneration effects following stress. The materials used in this study consisted of seedlings of three triticale lines differing in Al3+ tolerance, first subjected to aluminum ion stress and then recovered. Two-dimensional electrophoresis (2-DE) was used for seedling root protein separation followed by differential spot analysis using liquid chromatography coupled to tandem mass spectrometry (LC-MS-MS/MS). The plants’ tolerance to the stress was evaluated based on biometric screening of seedling root regrowth upon regeneration. Our results suggest that the Al-tolerant genotype can recover, without differentiation of proteome profiles, after stress relief, contrary to Al-sensitive genotypes that maintain the proteome modifications caused by unfavorable environments.

 

See https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8781804/pdf/plants-11-00165.pdf

 

Figure 2. Computational prediction of the functional network between differential proteins. The proteins used for analysis are presented in Tables 3 and 4. The number of connecting lines is in proportion to the amount of information about the protein interactions available. The line color indicates the type of interaction evidence. The explanation of symbols used in STRING database annotations are as follows: Traes_4BS_7AE61936D.1—oxalate oxidase; GST1—glutathione S-transferase; atp1— ATP synthase subunit alpha, mitochondrial; PER1— 1-Cys peroxiredoxin; Traes_3B_FC37FEAEE.2—protein disulfide-isomerase; U2AF65B—splicing factor U2af large subunit B; Traes_1DS_C327E495D.1—serpin-Z1C; Traes_7DL_6AC3E4622.2— eukaryotic initiation factor 4A; Traes_1BL_CB7AE51FA.1—calmodulin; Traes_1AS_36865F81C.2— ubiquitin; SHH—adenosylhomocysteinase; Traes_1AL_672A850FF.2—phosphoglycerate kinase, cytosolic; GLUD1—DIMBOA 1b, chloroplastic; TUBB3—tubulin beta-3 chain; TUBA— tubulin alpha chain; Traes_3AS_D1E1079AA1—S-adenosylmethionine synthase; VDAC1— mitochondrial outer membrane porin; FBP—fructose-1,6-bisphosphatase; COR410—dehydrin COR410; rpoB—DNA-directed RNA polymerase subunit beta; OMT1—flavone O-methyltransferase 1; Traes_2AL81CAF6C30.2—phosphomannomutase.

 

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