Identification of the glycerol-3-phosphate dehydrogenase (GPDH) gene family in wheat and its expression profiling analysis under different stress treatments
DOI:
https://doi.org/10.15835/nbha50312611Keywords:
abiotic stress, expression profile, glycerol-3-phosphate dehydrogenase (GPDH);, phylogeny, wheatAbstract
Glycerol-3-phosphate dehydrogenase (GPDH) catalyses the interconversion of glycerol-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), and plays key roles in different developmental processes and stress responses. GPDH family genes have been previously investigated in various plant species, such as Arabidopsis, maize, and soybean. However, very little is known in GPDH family genes in wheat. In this study, a total of 17 TaGPDH genes were identified from the wheat genome, including eight cytosolic GPDHs, six chloroplastic GPDHs and three mitochondrial GPDHs. Gene duplication analysis showed that segmental duplications contributed to the expansion of this gene family. Phylogenetic results showed that TaGPDHs were clustered into three groups with the same subcellular localization and domain distribution, and similar conserved motif arrangement and gene structure. Expression analysis based on the RNA-seq data showed that GPDH genes exhibited preferential expression in different tissues, and several genes displayed altered expression under various abiotic stresses. These findings provide the foundation for further research of wheat GPDH genes in plant growth, development and stress responses.
References
Borrill P, Ramirez-Gonzalez R, Uauy C. (2016). expVIP: a customizable RNA-seq data analysis and visualization platform. Plant Physiol 170(4):2172-2186. https://doi.org/10.1104/pp.15.01667
Casais-Molina ML, Peraza-Echeverria S, Echevarría-Machado I, Herrera-Valencia VA. (2016). Expression of Chlamydomonas reinhardtii CrGPDH2 and CrGPDH3 cDNAs in yeast reveals that they encode functional glycerol-3-phosphate dehydrogenases involved in glycerol production and osmotic stress tolerance. J Appl Phycol 28(1):219-226. https://doi.org/10.1007/s10811-015-0588-3
Chanda B, Xia Y, Mandal MK, Yu K, Sekine KT, Gao QM, … Kachroo P. (2011). Glycerol-3-phosphate is a critical mobile inducer of systemic immunity in plants. Nat Genet 43(5):421-427. https://doi.org/10.1038/ng.798
Chen H, Lao YM, Jiang JG. (2011). Effects of salinities on the gene expression of a NAD+-dependent glycerol-3-phosphate dehydrogenase in Dunaliella salina. Sci Total Environ 409(7):1291-1297. https://doi.org/10.1016/j.scitotenv.2010.12.038
Chen Z, Shen Z, Zhao D, Xu L, Zhang L, Zou Q. (2020). Genome-wide analysis of LysM-containing gene family in wheat: Structural and phylogenetic analysis during development and defense. Genes (Basel) 12(1):31. https://doi.org/10.3390/genes12010031
Chhikara S, Abdullah HM, Akbari P, Schnell D, Dhankher OP. (2018). Engineering Camelina sativa (L.) Crantz for enhanced oil and seed yields by combining diacylglycerol acyltransferase1 and glycerol-3-phosphate dehydrogenase expression. Plant Biotechnol J 16(5):1034-1045. https://doi.org/10.1111/pbi.12847
Driver T, Trivedi DK, McIntosh OA, Dean AP, Goodacre R, Pittman JK. (2017). Two glycerol-3-phosphate dehydrogenases from Chlamydomonas have distinct roles in lipid metabolism. Plant Physiol 174(4):2083-2097. https://doi.org/10.1104/pp.17.00491
Gholizadeh F, Mirzaghaderi G. (2020). Genome-wide analysis of the polyamine oxidase gene family in wheat (Triticum aestivum L.) reveals involvement in temperature stress response. PLoS One 15(8):e0236226. https://doi.org/10.1371/journal.pone.0236226
He Q, Toh JD, Ero R, Qiao Z, Kumar V, Serra A, … Gao YG. (2020). The unusual di-domain structure of Dunaliella salina glycerol-3-phosphate dehydrogenase enables direct conversion of dihydroxyacetone phosphate to glycerol. Plant J 102(1):153-164. https://doi.org/10.1111/tpj.14619
He X, Liu M, Fang Z, Ma D, Zhou Y, Yin JL. (2021). Genome-wide analysis of a plant at-rich sequence and zinc-binding protein (PLATZ) in Triticum Aestivum. Phyton-Int J Exp Bot 90:971-986. https://doi.org/10.32604/phyton.2021.012726
Herrera-Valencia VA, Macario-González LA, Casais-Molina ML, Beltran-Aguilar AG, Peraza-Echeverría S. (2012). In silico cloning and characterization of the glycerol-3-phosphate dehydrogenase (GPDH) gene family in the green microalga Chlamydomonas reinhardtii. Curr Microbiol 64(5):477-485. https://doi.org/10.1007/s00284-012-0095-6
Hu B, Jin J, Guo AY, Zhang H, Luo J, Gao G. (2015). GSDS 2.0: an upgraded gene feature visualization server. Bioinformatics 31(8):1296-1297. https://doi.org/10.1093/bioinformatics/btu817
Jin P, Gao S, He L, Xu M, Zhang T, Zhang F, … Chen J. (2020). Genome-wide identification and expression analysis of the histone deacetylase gene family in wheat (Triticum aestivum L.). Plants (Basel) 10(1):19. https://doi.org/10.3390/plants10010019
Kumar S, Stecher G, Tamura K. (2016). MEGA7: Molecular evolutionary genetics analysis version 7.0 for bigger datasets. Mol Biol Evol 33(7):1870-1874. https://doi.org/10.1093/molbev/msw054
Liao L, Hu Z, Liu S, Yang Y, Zhou Y. (2021). Characterization of germin-like proteins (GLPs) and their expression in response to abiotic and biotic stresses in cucumber. Horticulturae 7(10):412
Liu Z, Xin M, Qin J, Peng H, Ni Z, Yao Y, Sun Q. (2015). Temporal transcriptome profiling reveals expression partitioning of homeologous genes contributing to heat and drought acclimation in wheat (Triticum aestivum L.). BMC Plant Biol 15:152. https://doi.org/10.1186/s12870-015-0511-8
Lorenc-Kukula K, Chaturvedi R, Roth M, Welti R, Shah J. (2012). Biochemical and molecular-genetic characterization of SFD1's involvement in lipid metabolism and defense signaling. Front Plant Sci 3:26. https://doi.org/10.3389/fpls.2012.00026
Mráček T, Drahota Z, Houštěk J. (2013). The function and the role of the mitochondrial glycerol-3-phosphate dehydrogenase in mammalian tissues. Biochim Biophys Acta 1827(3):401-410. https://doi.org/10.1016/j.bbabio.2012.11.014
Nandi A, Welti R, Shah J. (2004). The Arabidopsis thaliana dihydroxyacetone phosphate reductase gene SUPPRESSSOR OF FATTY ACID DESATURASE DEFICIENCY1 is required for glycerolipid metabolism and for the activation of systemic acquired resistance. Plant Cell 16(2):465-477. https://doi.org/10.1105/tpc.016907
Shen W, Wei Y, Dauk M, Tan Y, Taylor DC, Selvaraj G, Zou J. (2006). Involvement of a glycerol-3-phosphate dehydrogenase in modulating the NADH/NAD+ ratio provides evidence of a mitochondrial glycerol-3-phosphate shuttle in Arabidopsis. Plant Cell 18(2):422-441. https://doi.org/10.1105/tpc.105.039750
Shen W, Wei Y, Dauk M, Zheng Z, Zou J. (2003). Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants. FEBS Lett 536(1-3):92-96. https://doi.org/10.1016/s0014-5793(03)00033-4
Singh V, Singh PK, Siddiqui A, Singh S, Banday ZZ, Nandi AK. (2016). Over-expression of Arabidopsis thaliana SFD1/GLY1, the gene encoding plastid localized glycerol-3-phosphate dehydrogenase, increases plastidic lipid content in transgenic rice plants. J Plant Res 129(2):285-293. https://doi.org/10.1007/s10265-015-0781-0
Vigeolas H, Geigenberger P. (2004). Increased levels of glycerol-3-phosphate lead to a stimulation of flux into triacylglycerol synthesis after supplying glycerol to developing seeds of Brassica napus L. in planta. Planta 219(5):827-835. https://doi.org/10.1007/s00425-004-1273-y
Vigeolas H, Waldeck P, Zank T, Geigenberger P. (2007). Increasing seed oil content in oil-seed rape (Brassica napus L.) by over-expression of a yeast glycerol-3-phosphate dehydrogenase under the control of a seed-specific promoter. Plant Biotechnol J 5(3):431-441. https://doi.org/10.1111/j.1467-7652.2007.00252.x
Voorrips RE. (2002). MapChart: software for the graphical presentation of linkage maps and QTLs. J Hered 93(1):77-78. https://doi.org/10.1093/jhered/93.1.77
Wei Y, Periappuram C, Datla R, Selvaraj G, Zou J. (2001). Molecular and biochemical characterizations of a plastidic glycerol-3-phosphate dehydrogenase from Arabidopsis. Plant Physiol Biochem 39(10):841-848. https://doi.org/https://doi.org/10.1016/S0981-9428(01)01308-0
Wu Q, Lan Y, Cao X, Yao H, Qiao D, Xu H, Cao Y. (2019). Characterization and diverse evolution patterns of glycerol-3-phosphate dehydrogenase family genes in Dunaliella salina. Gene 710:161-169. https://doi.org/10.1016/j.gene.2019.05.056
Xue LL, Chen HH, Jiang JG. (2017). Implications of glycerol metabolism for lipid production. Prog Lipid Res 68:12-25. https://doi.org/10.1016/j.plipres.2017.07.002
Zhao Y, Cao P, Cui Y, Liu D, Li J, Zhao Y, … Chen Q. (2021a). Enhanced production of seed oil with improved fatty acid composition by overexpressing NAD+-dependent glycerol-3-phosphate dehydrogenase in soybean. J Integr Plant Biol 63(6):1036-1053. https://doi.org/10.1111/jipb.13094
Zhao Y, Li X, Wang F, Zhao X, Gao Y, Zhao C, … Xu J. (2018). Glycerol-3-phosphate dehydrogenase (GPDH) gene family in Zea mays L.: Identification, subcellular localization, and transcriptional responses to abiotic stresses. PLoS One 13(7):e0200357. https://doi.org/10.1371/journal.pone.0200357
Zhao Y, Li X, Zhang Z, Pan W, Li S, Xing Y, … Chen Q. (2021b). GmGPDH12, a mitochondrial FAD-GPDH from soybean, increases salt and osmotic stress resistance by modulating redox state and respiration. Crop J 9(1):79-94. https://doi.org/https://doi.org/10.1016/j.cj.2020.05.008
Zhao Y, Liu M, He L, Li X, Wang F, Yan B, … Xu J. (2019a). A cytosolic NAD+-dependent GPDH from maize (ZmGPDH1) is involved in conferring salt and osmotic stress tolerance. BMC Plant Biol 19(1):16. https://doi.org/10.1186/s12870-018-1597-6
Zhao Y, Liu M, Wang F, Ding D, Zhao CJ, He L, … Xu JY. (2019b). The role of AtGPDHc2 in regulating cellular redox homeostasis of Arabidopsis under salt stress. J Integr Agr 18(6):1266-1279. https://doi.org/https://doi.org/10.1016/S2095-3119(18)62082-9

Downloads
Published
How to Cite
Issue
Section
License
Copyright (c) 2022 Chao WANG, Zixian ZHOU, Shan JIANG, Qiang LI, Licao CUI, Yong ZHOU

This work is licensed under a Creative Commons Attribution 4.0 International License.
License:
Open Access Journal:
The journal allows the author(s) to retain publishing rights without restriction. Users are allowed to read, download, copy, distribute, print, search, or link to the full texts of the articles, or use them for any other lawful purpose, without asking prior permission from the publisher or the author.