The Plastidial Glyceraldehyde-3-Phosphate Dehydrogenase Is Critical for Abiotic Stress Response in Wheat

Li, Xixi; Wei, Wenjie; Li, Fangfang; Zhang, Lin; Deng, Xia; Liu, Ying; Yang, Shushen

doi:10.3390/ijms20051104

Cited by 33 publications

(22 citation statements)

References 54 publications

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“…All the results suggest that over-expression of TaGApC2-6D enhanced drought tolerance in Arabidopsis plants. A similar finding was also verified in other TaGApDH [ 39 ].…”

Section: Discussionsupporting

confidence: 89%

Cytosolic TaGAPC2 Enhances Tolerance to Drought Stress in Transgenic Arabidopsis Plants

Zhang

Yang

2020

IJMS

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Drought is a major natural disaster that seriously affects agricultural production, especially for winter wheat in boreal China. As functional proteins, the functions and mechanisms of glyceraldehyde-3-phosphate dehydrogenase in cytoplasm (GAPCs) have remained little investigated in wheat subjected to adverse environmental conditions. In this study, we cloned and characterized a GAPC isoform TaGAPC2 in wheat. Over-expression of TaGApC2-6D in Arabidopsis led to enhanced root length, reduced reactive oxygen species (ROS) production, and elevated drought tolerance. In addition, the dual-luciferase assays showed that TaWRKY28/33/40/47 could positively regulate the expression of TaGApC2-6A and TaGApC2-6D. Further results of the yeast two-hybrid system and bimolecular fluorescence complementation assay (BiFC) demonstrate that TaPLDδ, an enzyme producing phosphatidic acid (PA), could interact with TaGAPC2-6D in plants. These results demonstrate that TaGAPC2 regulated by TaWRKY28/33/40/47 plays a crucial role in drought tolerance, which may influence the drought stress conditions via interaction with TaPLDδ. In conclusion, our results establish a new positive regulation mechanism of TaGAPC2 that helps wheat fine-tune its drought response.

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“…All the results suggest that over-expression of TaGApC2-6D enhanced drought tolerance in Arabidopsis plants. A similar finding was also verified in other TaGApDH [ 39 ].…”

Section: Discussionsupporting

confidence: 89%

Cytosolic TaGAPC2 Enhances Tolerance to Drought Stress in Transgenic Arabidopsis Plants

Zhang

Yang

2020

IJMS

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“…GAPCp1 is a GAPDH from wheat that directly interacts with the cytochrome b6-f complex iron sulfite subunit (Cytb6f) (in yeast two-hybrid and bimolecular complementation assays). The latter protein has a role in ROS scavenging and could be implicated in drought responses [ 60 ].…”

Section: Discussionmentioning

confidence: 99%

Deciphering the Binding of Salicylic Acid to Arabidopsis thaliana Chloroplastic GAPDH-A1

Pokotylo

Hellal

Bouceba

et al. 2020

IJMS

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Salicylic acid (SA) has an essential role in the responses of plants to pathogens. SA initiates defence signalling via binding to proteins. NPR1 is a transcriptional co-activator and a key target of SA binding. Many other proteins have recently been shown to bind SA. Amongst these proteins are important enzymes of primary metabolism. This fact could stand behind SA’s ability to control energy fluxes in stressed plants. Nevertheless, only sparse information exists on the role and mechanisms of such binding. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was previously demonstrated to bind SA both in human and plants. Here, we detail that the A1 isomer of chloroplastic glyceraldehyde 3-phosphate dehydrogenase (GAPA1) from Arabidopsis thaliana binds SA with a KD of 16.7 nM, as shown in surface plasmon resonance experiments. Besides, we show that SA inhibits its GAPDH activity in vitro. To gain some insight into the underlying molecular interactions and binding mechanism, we combined in silico molecular docking experiments and molecular dynamics simulations on the free protein and protein–ligand complex. The molecular docking analysis yielded to the identification of two putative binding pockets for SA. A simulation in water of the complex between SA and the protein allowed us to determine that only one pocket—a surface cavity around Asn35—would efficiently bind SA in the presence of solvent. In silico mutagenesis and simulations of the ligand/protein complexes pointed to the importance of Asn35 and Arg81 in the binding of SA to GAPA1. The importance of this is further supported through experimental biochemical assays. Indeed, mutating GAPA1 Asn35 into Gly or Arg81 into Leu strongly diminished the ability of the enzyme to bind SA. The very same cavity is responsible for the NADP+ binding to GAPA1. More precisely, modelling suggests that SA binds to the very site where the pyrimidine group of the cofactor fits. NADH inhibited in a dose-response manner the binding of SA to GAPA1, validating our data.

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“…As a housekeeping gene or protein, GAPDH is widely used as a control in real-time polymerase chain reaction (PCR) experiments. However, studies on GAPDH participating in the cellular response to water stress [10], oxidative stress [11] and apoptosis [12] demonstrated that GAPDH was subject to changes in many biological conditions and might be not stably expressed under stress conditions [13]. Therefore, GAPDH as an internal standard should be tailored to the nature of the study.…”

Section: Introductionmentioning

confidence: 99%

“…Recent studies indicate that GAPC could perform other functions in plants, which are not related to its catalytic activity. In addition, it has a central role in the abiotic stress response to cold [13], cadmium [17] and salt [14,18], and GAPC was suggested as a moonlighting (multifunctional) protein in plants [15].…”

Section: Introductionmentioning

confidence: 99%

Characterization of LcGAPC and its transcriptional response to salt and alkali stress in two ecotypes of Leymus chinensis (Trin.) Tzvelev

Meng

Yang

et al. 2020

Biotechnology & Biotechnological Equipment

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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a housekeeping protein which plays various roles in non-metabolic processes in addition to its role in glucose catabolism. There are several GAPDH isoforms in plant cells. In this study, we cloned the full-length cDNA encoding the isoform GAPC in two ecotypes of Leymus chinensis (Trin.) Tzvelev, gray-green type and yellow-green type. The LcGAPC sequence includes an open reading frame (ORF) of 1014 bp encoding 337 amino acids. The predicted molecular weight is 36.5 kDa, and the pI is 6.19. The mRNA expression of LcGAPC decreased at 24 h and then increased significantly after 7 d after 400 mmol/L NaCl stress. At 200 mmol/L mixed alkali stress (NaHCO 3 :Na 2 CO 3 ¼9:1), the LcGAPC expression level gradually increased as time increased in the two ecotypes of L. chinensis. The results suggested that LcGAPC is a stress-inducible gene that might play a role in the salt and alkali stress response. This study provided a basis to further study the mechanism of expression characteristics under salt and alkali stress conditions of L. chinensis. ARTICLE HISTORY

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The Plastidial Glyceraldehyde-3-Phosphate Dehydrogenase Is Critical for Abiotic Stress Response in Wheat

Cited by 33 publications

References 54 publications

Cytosolic TaGAPC2 Enhances Tolerance to Drought Stress in Transgenic Arabidopsis Plants

Cytosolic TaGAPC2 Enhances Tolerance to Drought Stress in Transgenic Arabidopsis Plants

Deciphering the Binding of Salicylic Acid to Arabidopsis thaliana Chloroplastic GAPDH-A1

Characterization of LcGAPC and its transcriptional response to salt and alkali stress in two ecotypes of Leymus chinensis (Trin.) Tzvelev

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