Changes in Some Carbon and Nitrogen Metabolism Enzymes in Field-Grown Wheat

Ulduza A Gurbanova; Shahniyar M Bayramov; Novruz M Guliev; Irada M Huseynova

doi:10.17485/IJST/v14i43.1128

Article

Changes in Some Carbon and Nitrogen Metabolism Enzymes in Field-Grown Wheat

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Indian Journal of Science and Technology

DOI: 10.17485/IJST/v14i43.1128

Year: 2021, Volume: 14, Issue: 43, Pages: 3237-3245

Original Article

Changes in Some Carbon and Nitrogen Metabolism Enzymes in Field-Grown Wheat

Ulduza A Gurbanova^1*, Shahniyar M Bayramov¹, Novruz M Guliev¹, Irada M Huseynova¹¹

¹Department of Fundamental Problems of Biological Productivity, Institute of Molecular Biology & Biotechnologies, National Academy of Sciences, 11 Izzat Nabiyev, AZ, 1073, Baku, Azerbaijan, Azerbaijan

*Corresponding Author
Email: [email protected]

Received Date:18 July 2021, Accepted Date:02 December 2021, Published Date:21 December 2021

This work is licensed under a Creative Commons Attribution 4.0 International License.

Abstract

Objective: The activities of alanine and aspartate aminotransferases, NADmalate dehydrogenase in the ontogenesis have been determined in leaves of durum wheat genotypes (Barakatli 95, Garagylchyg 2) with contrasting drought tolerance, cultivated under natural soil drought conditions. Methods/ analysis: Enzymatic activities of aspartate and alanine transferases, NADmalate dehydrogenase were determined spectrophotometrically (Ultrospec 3300 pro, Amersham, USA). Measurements were taken at 340 nm for 1 min and the obtained results were expressed as mmol mg-1*protein min-1. The unequal variance two-tailed Student’s t-test was applied for the analysis of the significance of differences between plants cultivated under irrigated and natural drought conditions. P 0.05 was considered statistically significant. We used three samples for each treatment and performed the analysis twice. Findings : In flag leaves of the drought-tolerant Barakatli 95 genotype, the alanine aminotransferase activity increased ~2.7 and ~2.2 fold compared to the drought-sensitive Garagylchyg 2 genotype, under irrigated and natural drought conditions. According to the results, catabolism of amino acids is faster in the drought-sensitive Garagylchyg 2 genotype compared to the droughttolerant Barakatli 95 genotype under stress. Although the activity of all three enzymes studied varies in parallel in the ontogenesis of flag leaves, it is mostly dependent on leaf water content during the day. Novelty/improvement: The obtained data suggest that high enzyme activities in the Barakati 95 genotype play a role in achieving drought tolerance.

Keywords: Wheat; flag leaf; natural drought conditions; aspartate aminotransferase; alanine aminotransferase; daytime

References

Baslam M, Mitsui T, Sueyoshi K, Ohyama T. Recent Advances in Carbon and Nitrogen Metabolism in C3 Plants. International Journal of Molecular Sciences. 2020;22(1):318. Available from: https://dx.doi.org/10.3390/ijms22010318
Dahal K, Wang J, Martyn GD, Rahimy F, Vanlerberghe GC. Mitochondrial Alternative Oxidase Maintains Respiration and Preserves Photosynthetic Capacity during Moderate Drought in Nicotiana tabacum. Plant Physiology. 2014;166(3):1560–1574. Available from: https://dx.doi.org/10.1104/pp.114.247866
Michae M, Ankerst DP, Annette M. Interactions between temperature and drought in global and regional crop yield variability during 1961-2014. PLoS One. 1961;12:178339. Available from: 10.1371/journal.pone.0178339
Ali R, Ali R, Saher MS, Xiling Z, Xuekun Z, Yan L. Xu Jinsong Impact of Climate Change on Crops Adaptation and Strategies to Tackle Its Outcome: A Review. Plants (Basel). 2019;8(2):34. doi: doi: 10.3390/plants8020034
Leng G, Hall J. Crop yield sensitivity of global major agricultural countries to droughts and the projected changes in the future. Science of The Total Environment. 2019;654:811–821. Available from: https://dx.doi.org/10.1016/j.scitotenv.2018.10.434
Batista‐Silva W, Heinemann B, Rugen N, Nunes‐Nesi A, Araújo WL, Braun H, et al. The role of amino acid metabolism during abiotic stress release. Plant, Cell & Environment. 2019;42(5):1630–1644. Available from: https://dx.doi.org/10.1111/pce.13518
Hildebrandt T, Nunes Nesi A, Araújo W, Braun HP. Amino Acid Catabolism in Plants. Molecular Plant. 2015;8(11):1563–1579. Available from: https://dx.doi.org/10.1016/j.molp.2015.09.005
Liszka A, Schimpf R, Zaruma KIC, Buhr A, Seidel T, Walter S, et al. Three cytosolic NAD-malate dehydrogenase isoforms of Arabidopsis thaliana: on the crossroad between energy fluxes and redox signaling. Biochemical Journal. 2020;477(19):3673–3693. Available from: https://dx.doi.org/10.1042/bcj20200240
McAllister CH, Good AG. Alanine Aminotransferase Variants Conferring Diverse NUE Phenotypes in Arabidopsis thaliana. PLOS ONE. 2015;10(4):e0121830. Available from: https://dx.doi.org/10.1371/journal.pone.0121830
Marcio R, Francesco L, Wagner LA, Adriano NN, Ladaslav S, FernieAlisdair, et al. Fernie Alisdair, and van Dongen Joost Glycolysis and the Tricarboxylic Acid Cycle Are Linked by Alanine Aminotransferase during Hypoxia Induced by Waterlogging of Lotus japonicas. Plant Physiology. 2010;152(3):1501–1513. Available from: https://doi.org/10.1104/pp.109.150045
Gaufichon L, Rothstein SJ, Suzuki A. Asparagine Metabolic Pathways in Arabidopsis. Plant and Cell Physiology. 2016;57(4):675–689. Available from: https://dx.doi.org/10.1093/pcp/pcv184
Guo R, Shi L, Ding X, Hu Y, Tian S, Yan D, et al. Effects of Saline and Alkaline Stress on Germination, Seedling Growth, and Ion Balance in Wheat. Agronomy Journal. 2010;102(4):1252–1260. Available from: https://dx.doi.org/10.2134/agronj2010.0022
Schertl P, Braun HP. Respiratory electron transfer pathways in plant mitochondria. Frontiers in Plant Science. 2014;5:163. Available from: https://dx.doi.org/10.3389/fpls.2014.00163
Galili G, Avin-Wittenberg T, Angelovici R, Fernie AR. The role of photosynthesis and amino acid metabolism in the energy status during seed development. Frontiers in Plant Science. 2014;5:447. Available from: https://dx.doi.org/10.3389/fpls.2014.00447
Naliwajski MR, Skłodowska M. The relationship between carbon and nitrogen metabolism in cucumber leaves acclimated to salt stress. Plant Biology. 2018;6:e6043. Available from: https://dx.doi.org/10.7717/peerj.6043
Alfonso SU, Brüggemann W. Photosynthetic responses of a C3 and three C4 species of the genus Panicum (s.l.) with different metabolic subtypes to drought stress. Photosynthesis Research. 2012;112(3):175–191. Available from: https://dx.doi.org/10.1007/s11120-012-9763-4
Tambussi EA, Nogués S, Araus JL. Ear of durum wheat under water stress: water relations and photosynthetic metabolism. Planta. 2005;221(3):446–458. Available from: https://dx.doi.org/10.1007/s00425-004-1455-7
Rekowski A, Langenkämper G, Dier M, Wimmer MA, Scherf KA, Zörb C. Determination of soluble wheat protein fractions using the Bradford assay. Cereal Chemistry. 2021;98(5):1059–1065. Available from: https://dx.doi.org/10.1002/cche.10447
Borst P. The malate–aspartate shuttle (Borst cycle): How it started and developed into a major metabolic pathway. IUBMB Life. 2020;72(11):2241–2259. Available from: https://dx.doi.org/10.1002/iub.2367
Easlon E, Tsang F, Skinner C, Wang C, Lin SJ. The malate–aspartate NADH shuttle components are novel metabolic longevity regulators required for calorie restriction-mediated life span extension in yeast. Genes & Development. 2008;22(7):931–944. Available from: https://dx.doi.org/10.1101/gad.1648308
Monné M, Miniero DV, Bisaccia F, Fiermonte G. The mitochondrial oxoglutarate carrier: from identification to mechanism. Journal of Bioenergetics and Biomembranes. 2013;45(1-2):1–13. Available from: https://dx.doi.org/10.1007/s10863-012-9475-7
Sousa CAFd, Sodek L. Alanine metabolism and alanine aminotransferase activity in soybean (Glycine max) during hypoxia of the root system and subsequent return to normoxia. Environmental and Experimental Botany. 2003;50(1):1–8. Available from: https://dx.doi.org/10.1016/s0098-8472(02)00108-9
Claudie R, Orcaray EL, Jean-Bernard C. Limami Anis M. Characterization of alanine aminotransferase (AlaAT) multigene family and hypoxic response in young seedlings of the model legume Medicago truncatula. Journal of Experimental Botany. 2006;57(12):3079–3089. doi: 10.1093/jxb/erl069
Miyashita Y, Dolferus R, Ismond KP, Good AG. Alanine aminotransferase catalyses the breakdown of alanine after hypoxia in Arabidopsis thaliana. The Plant Journal. 2007;49(6):1108–1121. Available from: https://dx.doi.org/10.1111/j.1365-313x.2006.03023.x
Xu Z, Ma J, Qu C, Hu Y, Hao B, Sun Y, et al. Identification and expression analyses of the alanine aminotransferase (AlaAT) gene family in poplar seedlings. Scientific Reports. 2017;7(1):45933. Available from: https://dx.doi.org/10.1038/srep45933
Driesen E, Ende WVD, Proft MD, Saeys W. Influence of Environmental Factors Light, CO2, Temperature, and Relative Humidity on Stomatal Opening and Development: A Review. Agronomy. 2020;10(12):1975. doi: 10.3390/agronomy10121975
Yongqiang C, Zhiyuan F, Hui Z, Runmiao T, Huili Y, Canran S, et al. Tang Jihua Cytosolic malate dehydrogenase 4 modulates cellular energetics and storage reserve accumulation in maize endosperm. Plant Biotechnology Journal. 2020;18(12). Available from: https://doi.org/10.1111/pbi.13416
Selinski J, Scheibe R. Malate valves: old shuttles with new perspectives. Plant Biology. 2019;21(S1):21–30. Available from: https://dx.doi.org/10.1111/plb.12869
Omini J, Wojciechowska I, Skirycz A, Moriyama H, Obata T. Association of the malate dehydrogenase-citrate synthase metabolon is modulated by intermediates of the Krebs tricarboxylic acid cycle. Scientific Reports. 2021;11(1):18770. Available from: https://dx.doi.org/10.1038/s41598-021-98314-z
Abir I, George R, Gupta K, Kapuganti J. Plant mitochondria: source and target for nitric oxide. Mitochondrion. 2014;19:329–333. doi: 10.1016/j.mito.2014.02.003
Tomaz T, Bagard M, Pracharoenwattana I, Lindén P, Lee CP, Carroll AJ, et al. Mitochondrial Malate Dehydrogenase Lowers Leaf Respiration and Alters Photorespiration and Plant Growth in Arabidopsis. Plant Physiology. 2010;154(3):1143–1157. doi: 10.1104/pp.110.161612
Häusler RE, Ludewig F, Krueger S. Amino acids – A life between metabolism and signaling. Plant Science. 2014;229:225–237. doi: 10.1016/j.plantsci.2014.09.011

Copyright

© 2021 Gurbanova et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Published By Indian Society for Education and Environment (iSee)