Nitrate assimilation pathway in higher plants: critical role in nitrogen signalling and utilization
DOI:
https://doi.org/10.14719/pst.2020.7.2.637Keywords:
carbon-nitrogen interaction, nitrate assimilation, nitrate transporters, nitrogen use efficiency, Ammonia assimilationAbstract
The process of nitrate assimilation is a very crucial pathway for the sustainable growth and productivity of higher plants. This process is catalysed by two enzymes, nitrate reductase and nitrite reductase. Both the enzymes differ from each other with respect to their structural organisation, subcellular location, catalytic efficiencies and regulatory mechanisms. Nitrate reductase catalyses the rate limiting step of nitrate assimilation process. The genes and proteins of this enzyme have been isolated and characterised from many higher plants. The additional role of NR in the production of nitric oxide has been also reported in last several years. The reduced ammonium is assimilated into carbon skeleton, ?-ketoglutarate, by the concerted action of glutamine synthetase and glutamate synthase. Glutamine and glutamate are the transportable forms of nitrogen among various tissues and metabolic processes. The rate of nitrate assimilation is regulated by the rate of uptake of nitrate by nitrate transporters, availability of carbon skeleton, accumulation of nitrogenous end products, light and the rate of photosynthesis. The partitioning of metabolites and resources between carbon and nitrogen metabolism is an important factor for the growth and yield of plants. During the last several decades excess use of nitrogen fertiliser has caused environmental pollution. Efforts have been made to increase the nitrogen use efficiency of plants to reduce the cost on fertiliser and nitrate pollution, increase the productivity and protein content of several commonly used crops. This review discusses the process of nitrate assimilation and its interaction with the carbon metabolism.
Downloads
Download data is not yet available.
References
1. Wang LX, Macko SA. Constrained preferences in nitrogen uptake across plant species and environments. Plant Cell Environ. 2011;34:525-34. https://doi.org/10.1111/j.1365-3040.2010.02260.x
2. Wang Ya-Yun, Cheng Yu-Hsuan, Chen Kuo-En, Tsay Yi-Fang. Nitrate transport, signaling, and use efficiency. Annu Rev Plant Biol. 2018;69:85-122. https://doi.org/10.1146/annurev-arplant-042817-040056
3. Qu CP, Xu ZR, Hu YB, Lu Y, Yang CJ, Sun GY, et al. RNA-SEQ Reveals Transcriptional Level Changes of Poplar Roots in Different Forms of Nitrogen Treatments. Front Plant Sci. 2016;7:51. https://doi.org/10.3389/fpls.2016.00051
4. Nasholm T, Keilland K, Ganeteg U. Uptake of uptake or organic nitrogen by plants. New Phytol. 2009;182:31-48. https://doi.org/10.1111/j.1469-8137.2008.02751.x
5. Ali A, Sivakami S, Raghuram N. Regulation of activity and transcript levels of NR in Rice (Oryza sativa): Roles of Protein Kinase and G-proteins. Plant Sci. 2007;172:406-13. http://doi.org/10.1016/j.plantsci.2006.10.003
6. Lea PJ, Ireland RJ. Nitrogen metabolism in higher plants. In: Singh, BK, editor. Plant amino acids. biochemistry and biotechnology. New York: Marcel Dekker; 1999. p. 1–47.
7. Goel P, Singh AK. Abiotic stresses down regulate key genes involved in nitrogen uptake and assimilation in Brassica juncea L. PLoSONE. 2015;10:e0143645. https://doi:10.1371/journal.pone.0143645
8. Wang R, Liu D, Crawford NM. The Arabidopsis CHL1 protein plays a major role in high-affinity nitrate uptake. Proc Natl Acad Sci USA. 1998;95:15134-39. https://doi.org/10.1073/pnas.95.25.15134
9. Forde BG. Local and long-range signaling pathways regulating plant responses to nitrate. Annu Rev Plant Biol. 2002;53:203-24. https://doi.org/10.1146/annurev.arplant.53.100301.135256
10. Glass ADM. Nitrate uptake by plant roots. Botany. 2009;87:659–67. https://doi.org/10.1139/B09-014
11. Galvan A, Fernandez E. Eukaryotic nitrate and nitrite transporters. Cell Mol Life Sci. 2001;58:225–33. https://doi.org/10.1007/PL00000850
12. Kiba T, Krapp A. Plant nitrogen acquisition under low availability: Regulation of uptake and root architecture. Plant Cell Physiol. 2016;57:707–14. https://doi.org/10.1093/pcp/pcw052
13. Crawford NM, Glass ADM. Molecular and physiological aspects of nitrate uptake in plants. Trends Plant Sci. 1998;3:389–95. http://doi.org/10.1016/S1360-1385(98)01311-9
14. Aslam M, Travis R, Huffaker R. Comparative kinetics and reciprocal inhibition of nitrate and nitrite uptake in roots of uninduced and induced barley (Hordeum vulgare L.) Seedlings. Plant Physiol. 1992;99:1124–33. https://doi.org/10.1104/pp.99.3.1124
15. Glass ADM, Shaff JE, Kochian LV. Studies of the uptake of nitrate in barley. IV. Electrophysiology. Plant Physiol. 1992; 99:456–63. http://doi.org/ 10.1104/pp.99.2.456
16. Siddiqi MY, Glass ADM, Ruth TJ, Rufty TW Jr. Studies of the uptake of nitrate in barley. Plant Physiol. 1990;93:1426–32. https://doi.org/10.1104/pp.93.4.1426
17. Chrispeels MJ, Crawford NM, Schroeder JI. Proteins for transport of water and mineral nutrients across the membranes of plant cells. Plant Cell. 1999;11(4):661–76. http://doi.org/10.1105/tpc.11.4.661
18. Kronzucker HJ, Siddiqi MY, Glass ADM. Kinetics of NO3- influx in spruce. Plant Physiol. 1995;109:319–26. https://doi.org/10.1104/pp.109.1.319
19. Forde BG. Nitrate transporters in plants: structure, function and regulation. Biochim Biophys Acta. 2000;1465:219-35. https://doi.org/10.1016/S0005-2736(00)00140-1
20. Lin C-M, Koh S, Stacey G, Yu SM, Lin TY, Tsay YF. Cloning and functional characterization of a constitutively expressed nitrate transporter gene, osnrt1, from Rice. Plant Physiol. 2000;122:379-88. https://doi.org/10.1104/pp.122.2.379
21. Kronzucker HJ, Glass ADM, Siddiqi MY. Inhibition of nitrate uptake by ammonium in barley. Analysis of component fluxes. Plant Physiol. 1999;120:283–91. https://doi.org/10.1104/pp.120.1.283
22. Muller B, Touraine B. Inhibition of NO3- uptake by various phloem-translocated amino acids in soybean seedlings. J Exp Bot. 1992;43:617–23. http://doi.org/10.1093/jxb/43.5.617
23. Crawford NM, Forde BG. Molecular and developmental biology of inorganic nitrogen nutrition. Arabidopsis Book. 2002;1:e0011. http://doi.org/10.1199/tab.0011
24. derLeij M, Smith SJ, Miller AJ. Remobilization of vacuolar stored nitrate in barley root cells. Planta. 1998;205:64–72. https://doi.org/10.1007/s004250050297
25. Faure JD, Meyer C, Caboche M. Nitrate assimilation: nitrate and nitrite reductases. In: Morot-Gaudry JF, editor. Nitrogen assimilation by plants. Enfield: Science Publishers Inc; 2001. p. 33–52.
26. Brunswick P, Cresswell CF. Nitrite uptake into intact pea chloroplasts: II. Influence of electron transport regulators, uncouplers, ATPase and anion uptake inhibitors and protein binding reagents. Plant Physiol. 1988;86:384-89. https://doi.org/10.1104/pp.86.2.384
27. Shingles R, Roh MH, McCarty RE. Nitrite transport in chloroplast inner envelope vesicles. I. Direct measurement of proton-linked transport. Plant Physiol. 1996;112:1375-81. https://doi.org/10.1104/pp.112.3.1375
28. Sugiura M, Georgescu MN, Takahashi M. A nitrite transporter associated with nitrite uptake by higher plant chloroplasts. Plant Cell Physiol. 2007;48:1022–35. https://doi.org/10.1093/pcp/pcm073
29. Campbell WH. Nitrate reductase, structure, function and regulation: Bridging the gap between biochemistry and physiology. Annu Rev Plant Physiol Plant Mol Biol. 1999;50:277-303. https://doi.org/10.1146/annurev.arplant.50.1.277
30. Friemann A, Brinkmann K, Hachtel W. Sequence of a cdna encoding bi-specific NAD(P)H-nitrate reductase from the tree Betula pendula and identification of conserved protein regions. Mol Gen Genomics. 1991;227:97-105. http://doi..org/10.1007/bf00260713
31. Zhou J, Kleinhofs A. Molecular evolution of nitrate reductase genes. J Mol Evol. 1996;42:432-42. https://doi.org/10.1007/BF02498637
32. Schondorf T, Hachtel W. The choice of reducing substrate is altered by replacement of an alanine by proline in the FAD domain of a bispecific NADH(P)H-nitrate reductase from birch. Plant Physiol. 1995;108:203-10. https://doi.org/10.1104/pp.108.1.203
33. Campbell WH. Molecular control of nitrate reductase and other enzymes involved in nitrate assimilation. In: Foyer CH, Noctor G, editors. Photosynthetic nitrogen assimilation and associated carbon and respiratory metabolism. Dordecht: Kluwer Academic Publishers; 2002. p. 35-48. https://doi.org/10.1007/0-306-48138-3_3
34. Campbell WH. Nitrate reductase biochemistry comes of age. Plant Physiol. 1996;111:355-61. https://doi.org/10.1104/pp.111.2.355
35. Schwarz G, Mendel RR. Molybdenum cofactor biosynthesis and molybdenum enzymes. Annu Rev Plant Biol. 2006;57:623-47. https://doi.org/10.1146/annurev.arplant.57.032905.105437
36. Kamachi K, Amemiya Y, Ogura N, Nakagawa H. Immuno-gold localization of nitrate reductase in spinach (Spinacea oleracea) leaves. Plant Cell Physiol. 1987;28:333-38. https://doi.org/10.1093/oxfordjournals.pcp.a077300
37. Solomonson LP, Barber MJ. Assimilatory nitrate reductase: functional properties and regulation. Annu Rev Plant Physiol Plant Mol Biol. 1990;41:225-53. https://doi.org/10.1146/annurev.pp.41.060190.001301
38. Yamasaki H, Sakihama Y. Simultaneous production of nitric oxide and peroxynitrite by nitrate reductase: in vitro evidence for the NR-dependent formation of active nitrogen species. FEBS Lett. 2000;468:89-92. http://doi.org/10.1016/s0014-5793(00)01203-5
39. Chamizo-Ampudia A, Sanz-Luque E, Llamas A, Galvan A, Fernandez E. Nitrate Reductase Regulates Plant Nitric Oxide Homeostasis. Trends Plant Sci. 2017;22:163–74. DOI:10.1016/j.tplants.2016.12.001
40. Rockel P, Strube F, Rockel A, Wildt J, Kaiser WM. Regulation of nitric oxide (NO) production by plant nitrate reductase in vivo and in vitro. J Exp Bot. 2002;53:103-10. https://doi.org/10.1093/jexbot/53.366.103
41. Stöhr C, Strube P, Marx G, Ullrich, WR, Rockel P. A plasma-membrane-bound enzyme of tobacco or roots catalyses the formation of nitric oxide from nitrite. Planta. 2001;212:835-41. https://doi.org/10.1007/s004250000447
42. Prochazkova D, Haisel D, Pavlikova D. Nitric oxide biosynthesis in plants—the short overview. Plant Soil Environ. 2014;60:129–34. https://doi.org/10.17221/901/2013-PSE
43. Oaks A, Hirel B. Nitrogen Metabolism in roots. Annu Rev Plant Physiol. 1985;36:345-65. https://doi.org/10.1146/annurev.pp.36.060185.002021
44. Schuster C, Mohr H. Photooxidative damage to plastids affects the abundance of nitrate reductase mRNA in mustard cotyledons. Planta. 1990;181:125-28. https://doi.org/10.1007/BF00202334
45. Schuster C, Mohr H. Appearance of nitrite reductase mRNA in mustard seedling cotyledons is regulated by phytochrome. Planta. 1990;181:327-34. https://doi.org/10.1007/BF00195884
46. Yoneyama T, Suzuki A. Exploration of nitrate-to-glutamate assimilation in non-photosynthetic roots of higher plants by studies of (15)N-tracing, enzymes involved, reductant supply, and nitrate signaling: A review and synthesis. Plant Physiol Biochem. 2019;136:245–54. https://doi.org/10.1016/j.plaphy.2018.12.011
47. Bowsher CG, Hucklesby DP, Emes MJ. Induction of ferredoxin-NADP+oxidoreductase and ferredoxin synthesis in pea root plastids during nitrate assimilation. Plant J. 1993;3:463-67. https://doi.org/10.1111/j.1365-313X.1993.tb00166.x
48. Hase T, Schürmann P, Knaff DB. The interaction of ferredoxin with ferredoxin-dependent enzymes. In: Golbeck J, editor. Photosystem 1. Dordrecht, The Netherlands: Springer; 2006. p. 477–98. https://doi.org/10.1007/978-1-4020-4256-0_28
49. Fariduddin Q, Varshney P, Ali A. Perspective of nitrate assimilation and bioremediation in Spirulina platensis (a non-nitrogen fixing cyanobacterium): An overview. J Env Biol. 2018;39:547-57. http://doi.org/10.22438/jeb/39/5/MS-172
50. Sivasankar S, Rothstein S, Oaks A. Regulation of the accumulation and reduction of nitrate by nitrogen and carbon metabolites in maize seedlings. Plant Physiol. 1997;114:583-89. https://doi.org/10.1104/pp.114.2.583.
51. Maia LB, Moura JGJ. How biology handles nitrite. Chem. Rev. 2014;114:5273-357. https://doi.org/10.1021/cr400518y
52. Duncanson E, Gilkes AF, Kirk DW, Sheman A, Wray JL. Niri, a conditional-lethal mutant in barley causing a defect in nitrite reduction. Mol Gen Genet. 1993;236:275-82. https://doi.org/10.1007/BF00277123
53. Kishorekumar R, Bulle M, Wany A, Gupta KJ. An Overview of Important Enzymes Involved in Nitrogen Assimilation of Plants. In: Gupta K. Editor. Nitrogen Metabolism in Plants. Methods in Molecular Biology, 2020; vol 2057. New York Humana. https://doi.org/10.1007/978-1-4939-9790-9_1
54. Coruzzi GM. Primary N-assimilation into Amino Acids in Arabidopsis. The Arabidopsis Book. 2003;2:e0010. http://doi.org10.1199/tab.0010
55. Melo-Oliveira R, Cinha-Oliveira I, Coruzzi GM. Arabidopsis mutant analysis and gene regulation define a non-redundant role for glutamate dehydrogenase in nitrogen assimilation. Proc Natl Acad Sci USA. 1996;96:4718-23. https://doi.org/10.1073/pnas.93.10.4718
56. Anjana, Umar S, Iqbal M. Nitrate accumulation in plants, factors affecting the process, and human health implications. A review. Agron Sustain Dev. 2007;27:45-57. https://doi.org/10.1051/agro:2006021
57. Secheley KA, Yamata T, Oaks A. Compartmentation of nitrogen assimilation in higher plants. Int Rev Cyt. 1992;134:85-163. https://doi.org/10.1016/S0074-7696(08)62028-8
58. Cren M, Hirel B. Glutamine synthetase in higher plants: Regulation of gene and protein expression from the organ to the cell. Plant Cell Physiol. 1999;40:1187-93. https://doi.org/10.1093/oxfordjournals.pcp.a029506
59. Inokuchi R, Kuma K, Miyata T, Okada M. Nitrogen-assimilating enzymes in land plants and algae: phylogenic and physiological perspectives. Physiol Plant. 2002;116:1-11. https://doi.org/10.1034/j.1399-3054.2002.1160101.x
60. Lam HM, Coschigano KT, Oliveira IC, Melo-Oliveira R, Coruzzi GM. The molecular genetics of nitrogen assimilation into amino acids in higher plants. Annu Rev Plant Physiol Plant Mol Biol. 1996;47:569-93. https://doi.org/10.1146/annurev.arplant.47.1.569
61. Masclaux-Daubresse C, Daniel-Vedele F, Dechorgnat J, Chardon F, Gaufichon L, Suzuki A., Nitrogen uptake, assimilation and remobilization in plants: challenges for sustainable and productive agriculture, Annals Bot. 2010;105:1141–57. https://doi.org/10.1093/aob/mcq028
62. Suzuki A, Knaff DB. Glutamate synthase: structural, mechanistic and regulatory properties, and role in the amino acid metabolism. Photosynth Res. 2005;83:191-217. https://doi.org/10.1007/s11120-004-3478-0
63. Temple SJ, Vance CP, Gantt JS. Glutamate synthase and nitrogen assimilation. Trends Plant Sci. 1998;3:51-56. https://doi.org/10.1016/S1360-1385(97)01159-X
64. Forde B, Lea P. Glutamate in plants: Metabolism, regulation, and signalling. J Exp Bot. 2007; 58:2339-58. https://doi.org/10.1093/jxb/erm121
65. Hayakawa T, Nakamura T, Hattori F, Mae T, Ojima K, Yamaya T. Cellular localization of NADH-dependent glutamate synthase protein in vascular bundles of unexpanded leaf blades and young grains of rice plants. Planta. 1994;193:455-60. https://doi.org/10.1007/BF00201826
66. Coshigano KT, Melo-Oliveira R, Lim J, Coruzzi GM. Arabidopsis gls mutants and distinct Fd-GOGAT genes: implication for photorespiration and primary nitrogen assimilation. Plant Cell. 1998;10:741-52. https://doi.org/10.1105/tpc.10.5.741
67. Hirasawa M, Hurley JK, Salamon Z, Tollin G, Knaff DB. Oxidation-reduction and transient kinetics of ferredoxin dependent glutamate synthase. Arch Biochem Biophys. 1996; 330: 209-15. https://doi.org/10.1006/abbi.1996.0244
68. Sakakibara H, Kawabata S, Hase T, Sugiyama T. Differential effect of nitrate and light on the expression of glutamine synthetase and ferredoxin-dependent glutamate synthase in maize. Plant Cell Physiol. 1992;33:1193-98. https://doi.org/10.1093/oxfordjournals.pcp.a078373
69. Migge A, Carrayol E, Hirel B, Lohmann M, Meya G, Becker TW. Influence of UV-A or UV-B light and of the nitrogen source on the induction of ferredoxin-dependent glutamate synthase in etiolated tomato cotelydons. Plant Physiol Biochem. 1998;36:789-97. https://doi.org/10.1016/S0981-9428(99)80015-1
70. Hecht U, Oelmuller R, Schmidt S, Mohr H. Action of light, nitrate and ammonium on the levels of NADH- and ferredoxin-dependent glutamate synthase in the cotyledons of mustard seedlings. Planta. 1988;175:130-38. https://doi.org/10.1007/BF00402890
71. Yamaya T, Hayakawa T, Tanasawa K, Kamachi K, Mae T, Ojima K. Tissue distribution of glutamate synthase and glutamine synthetase in rice leaves. Occurrence of NADH-dependent glutamate synthase protein and activity in the unexpanded non-green leaf blades. Plant Physiol. 1992;100:1427-32. https://doi.org/10.1104/pp.100.3.1427
72. Kubik-Dobasz G. The activity of NADH, NADPH and ferredoxin-dependent glutamate synthase in the plastids and cytosol of Pisum arvense L. root cells. Acta Societatis Botanicorum Poloniae. 1989;58:253–62. https://doi.org/10.5586/asbp.1989.021
73. Rus-Alvarez A, Guerrier G. Proline metabolic pathways in calli from Lycopersicum esculentum and L. Pennellii under salt stress. Biol Plant (Prague). 1994;36:277-84. https://doi.org/10.1007/BF02921101
74. Foyer CH, Ferrario S. Modulation of carbon and nitrogen metabolism in transgenic plants with a view to improved biomass production. Biochem Soc Transac. 1994;22:909-15. https://doi.org/10.1042/bst0220909
75. Oliveira IC, Brenner E, Chiu J, Hsieh M-H, Kouranov A, Lam H-M, Shin MJ, Coruzzi G. Metabolite and light regulation of metabolism in plants: lessons from the study of a single biochemical pathway. Braz J Med Biol Res. 2001;34:567-75. http://dx.doi.org/10.1590/S0100-879X2001000500003
76. Kant S, Seneweera S, Rodin J, Materne M, Burch D, Rothstein SJ, Spangenberg G. Improving yield potential in crops under elevated CO2: integrating the photosynthetic and nitrogen utilization efficiencies. Front Plant Sci. 2012;3:162. https://doi.org/10.3389/fpls.2012.00162
77. Kaiser WM, Kandlbinder A, Stoimenova M, Glaab J. Discrepancy between nitrate reduction rates in intact leaves and nitrate reductase activity in leaf extracts: what limits nitrate reduction in situ? Planta. 2000;210:801–07. https://doi.org/10.1007/s004250050682
78. Xu G, Fan X, Miller AJ. Plant nitrogen assimilation and use efficiency. Annu Rev Plant Biol. 2012;63:153–82. https://doi.org/10.1146/annurev-arplant-042811-105532
79. Foyer C, Ferario-Mery S, Noctor G. Interactions between carbon and nitrogen metabolism. In: Lea PJ, Morot-Gaudry JF, editors. Plant nitrogen. Berlin: Springer Verlag; 2001. p. 237–54. https://doi.org/10.1007/978-3-662-04064-5_9
80. Li H, Liang Z, Ding G, Shi L, Xu F, Cai H. A Natural Light/Dark Cycle Regulation of Carbon-Nitrogen Metabolism and Gene Expression in Rice Shoots. Front Plant Sci. 2016;7:1318. https://doi.org/10.3389/fpls.2016.01318
81. Scheible WR, Gonzales-Fontes A, Morcuende R, Lauerer M, Geiger M, Glaab J, Schulze E-D, Stitt M. Tobacco mutants with a decreased number of functional nia-genes compensate by modifying the diurnal regulation transcription, post-translational modification and turnover of nitrate reductase. Planta. 1997;203:305–19. https://doi.org/10.1007/s004250050196
82. Lewis E, Noctor G, Causton D, Foyer CH. Regulation of assimilate partitioning in leaves. Aust J Plant Physiol. 2000; 27: 507-17. https://doi.org/10.1071/PP99177
83. Aslam M, Huffaker RC, Rains DW, Rao KP. Influence of light and ambient carbon dioxide concentration on nitrate assimilation by intact barley seedlings. Plant Physiol. 1979;63:1205-09. https://doi.org/10.1104/pp.63.6.1205
84. Nunes-Nesi A, Fernie AR, Stitt M. Metabolic andsignaling aspects underpinning the regulation of plant carbon nitrogen interactions. Mol Plant. 2010;3:973–96. https://doi.org/10.1093/mp/ssq049
85. Emes MJ, Neuhaus HE. Metabolism and transport in non-photosynthetic plastids. J Exp Bot. 1997;48:1995-2005. https://doi.org/10.1093/jxb/48.12.1995
86. Banks FM, Driscoll SP, Parry MAJ, Lawlor DW, Knight JS, Gray JC, et al. Decrease in phosphoribulokinase activity by antisense RNA in transgenic tobacco: relationship between photosynthesis, growth, and allocation at contrasting nitrogen supplies. Plant Physiol. 1999;119:1125-36. https://doi.org/10.1104/pp.119.3.1125
87. Morcuende R, Krapp A, Hurry V, Stitt M. Sucrose feeding leads to increased rates of nitrate assimilation, increased rates of oxoglutarate synthesis, and increased synthesis of a wide spectrum of amino acids in tobacco leaves. Planta. 1998;206:394–409. https://doi.org/10.1007/s004250050415
88. Amory AM, Vanlerberghe GC, Turpin DH. Demonstration of both a photosynthetic and nonphotosynthetic CO2 requirement for NH4+ assimilation in the green alga Selenastrumminutum. Plant Physiol. 1991;95:192-96. https://doi.org/10.1104/pp.95.1.192
89. Elrifi IR, Holmes JJ, Weger HG, Mayo WP, Turpin DH. Rubp limitation of photosynthetic carbon fixation during NH3 assimilation. Interactions between photosynthesis, respiration, and ammonium assimilation in N-limited green algae. Plant Physiol. 1988;87:395-401.https://doi.org/10.1104/pp.87.2.395
90. Pace GM, Volk RJ, Jackson WA. Nitrate reduction in response to CO2-1imited photosynthesis. Relationship to carbohydrate supply and nitrate reductase activity in maize seedlings. Plant Physiol. 1990;92:286-92. https://doi.org/10.1104/pp.92.2.286
91. Galangau F, Daniel-VedBle F, Moureaux T, Dorbe MF, Leydecker MT, Caboche M. Expression of leaf nitrate reductase genes from tomato and tobacco in relation to light dark regimes and nitrate supply. Plant Physiol. 1988;88:383-88. https://doi.org/10.1104/pp.88.2.383
92. Stitt M, Krapp A. The interaction between elevated carbon dioxide and nitrogen nutrition: the physiological and molecular background. Plant Cell Environ. 1999;22:583–621. https://doi.org/10.1046/j.1365-3040.1999.00386.x
93. Rufty TW, Mackown CT, Volk RJ. Effects of altered carbohydrate availability on whole-plant assimilation of 15NO3-. Plant Physiol. 1989;89:457-63. https://doi.org/10.1104/pp.89.2.457
94. Le VQ, Foyer C, Champigny ML. Effect of light and NO3- on wheat leaf phosphoenolpyruvate carboxylase activity. Plant Physiol. 1991;97):1476-82. https://doi.org/10.1104/pp.97.4.1476
95. Vanlerberghe GC, Schuller KA, Smith RG, Feil R, Plaxton WC, Turpin, DH. Relationship between NH4+ assimilation rate and in vivo phosphoenolpyruvate carboxylase activity. Plant Physiol. 1990;94:284-290. https://doi.org/10.1104/pp.94.1.284
96. Krapp A. Plant nitrogen assimilation and its regulation: A complex puzzle with missing pieces. Curr Opin Plant Biol. 2015;25:115–22. https://doi.org/10.1016/j.pbi.2015.05.010
97. Lammerts van Bueren ET, Struik PC. Diverse concepts of breeding for nitrogen use efficiency. A review. Agron Sustain Dev. 2017;37:50. https://doi.org/10.1007/s13593-017-0457-3
98. Andrews M, Lea PJ, Raven JA, Lindsey K. Can genetic manipulation of plant nitrogen assimilation enzymes result in increased crop yield and greater N-use efficiency? An assessment. Annals App Biol. 2004;145:25-40. https://doi.org/10.1111/j.1744-7348.2004.tb00356.x
99. Hachiya T, Sakakibara H. Interactions between nitrate and ammonium in their uptake, allocation, assimilation, and signaling in plants. J Exp Bot. 2017;68:2501–12, https://doi.org/10.1093/jxb/erw449
100. Britto DT, Kronzucker HJ. NH4+ toxicity in higher plants: a critical review. J Plant Physiol. 2002;159:567-84.https://doi.org/10.1078/0176-1617-0774
2. Wang Ya-Yun, Cheng Yu-Hsuan, Chen Kuo-En, Tsay Yi-Fang. Nitrate transport, signaling, and use efficiency. Annu Rev Plant Biol. 2018;69:85-122. https://doi.org/10.1146/annurev-arplant-042817-040056
3. Qu CP, Xu ZR, Hu YB, Lu Y, Yang CJ, Sun GY, et al. RNA-SEQ Reveals Transcriptional Level Changes of Poplar Roots in Different Forms of Nitrogen Treatments. Front Plant Sci. 2016;7:51. https://doi.org/10.3389/fpls.2016.00051
4. Nasholm T, Keilland K, Ganeteg U. Uptake of uptake or organic nitrogen by plants. New Phytol. 2009;182:31-48. https://doi.org/10.1111/j.1469-8137.2008.02751.x
5. Ali A, Sivakami S, Raghuram N. Regulation of activity and transcript levels of NR in Rice (Oryza sativa): Roles of Protein Kinase and G-proteins. Plant Sci. 2007;172:406-13. http://doi.org/10.1016/j.plantsci.2006.10.003
6. Lea PJ, Ireland RJ. Nitrogen metabolism in higher plants. In: Singh, BK, editor. Plant amino acids. biochemistry and biotechnology. New York: Marcel Dekker; 1999. p. 1–47.
7. Goel P, Singh AK. Abiotic stresses down regulate key genes involved in nitrogen uptake and assimilation in Brassica juncea L. PLoSONE. 2015;10:e0143645. https://doi:10.1371/journal.pone.0143645
8. Wang R, Liu D, Crawford NM. The Arabidopsis CHL1 protein plays a major role in high-affinity nitrate uptake. Proc Natl Acad Sci USA. 1998;95:15134-39. https://doi.org/10.1073/pnas.95.25.15134
9. Forde BG. Local and long-range signaling pathways regulating plant responses to nitrate. Annu Rev Plant Biol. 2002;53:203-24. https://doi.org/10.1146/annurev.arplant.53.100301.135256
10. Glass ADM. Nitrate uptake by plant roots. Botany. 2009;87:659–67. https://doi.org/10.1139/B09-014
11. Galvan A, Fernandez E. Eukaryotic nitrate and nitrite transporters. Cell Mol Life Sci. 2001;58:225–33. https://doi.org/10.1007/PL00000850
12. Kiba T, Krapp A. Plant nitrogen acquisition under low availability: Regulation of uptake and root architecture. Plant Cell Physiol. 2016;57:707–14. https://doi.org/10.1093/pcp/pcw052
13. Crawford NM, Glass ADM. Molecular and physiological aspects of nitrate uptake in plants. Trends Plant Sci. 1998;3:389–95. http://doi.org/10.1016/S1360-1385(98)01311-9
14. Aslam M, Travis R, Huffaker R. Comparative kinetics and reciprocal inhibition of nitrate and nitrite uptake in roots of uninduced and induced barley (Hordeum vulgare L.) Seedlings. Plant Physiol. 1992;99:1124–33. https://doi.org/10.1104/pp.99.3.1124
15. Glass ADM, Shaff JE, Kochian LV. Studies of the uptake of nitrate in barley. IV. Electrophysiology. Plant Physiol. 1992; 99:456–63. http://doi.org/ 10.1104/pp.99.2.456
16. Siddiqi MY, Glass ADM, Ruth TJ, Rufty TW Jr. Studies of the uptake of nitrate in barley. Plant Physiol. 1990;93:1426–32. https://doi.org/10.1104/pp.93.4.1426
17. Chrispeels MJ, Crawford NM, Schroeder JI. Proteins for transport of water and mineral nutrients across the membranes of plant cells. Plant Cell. 1999;11(4):661–76. http://doi.org/10.1105/tpc.11.4.661
18. Kronzucker HJ, Siddiqi MY, Glass ADM. Kinetics of NO3- influx in spruce. Plant Physiol. 1995;109:319–26. https://doi.org/10.1104/pp.109.1.319
19. Forde BG. Nitrate transporters in plants: structure, function and regulation. Biochim Biophys Acta. 2000;1465:219-35. https://doi.org/10.1016/S0005-2736(00)00140-1
20. Lin C-M, Koh S, Stacey G, Yu SM, Lin TY, Tsay YF. Cloning and functional characterization of a constitutively expressed nitrate transporter gene, osnrt1, from Rice. Plant Physiol. 2000;122:379-88. https://doi.org/10.1104/pp.122.2.379
21. Kronzucker HJ, Glass ADM, Siddiqi MY. Inhibition of nitrate uptake by ammonium in barley. Analysis of component fluxes. Plant Physiol. 1999;120:283–91. https://doi.org/10.1104/pp.120.1.283
22. Muller B, Touraine B. Inhibition of NO3- uptake by various phloem-translocated amino acids in soybean seedlings. J Exp Bot. 1992;43:617–23. http://doi.org/10.1093/jxb/43.5.617
23. Crawford NM, Forde BG. Molecular and developmental biology of inorganic nitrogen nutrition. Arabidopsis Book. 2002;1:e0011. http://doi.org/10.1199/tab.0011
24. derLeij M, Smith SJ, Miller AJ. Remobilization of vacuolar stored nitrate in barley root cells. Planta. 1998;205:64–72. https://doi.org/10.1007/s004250050297
25. Faure JD, Meyer C, Caboche M. Nitrate assimilation: nitrate and nitrite reductases. In: Morot-Gaudry JF, editor. Nitrogen assimilation by plants. Enfield: Science Publishers Inc; 2001. p. 33–52.
26. Brunswick P, Cresswell CF. Nitrite uptake into intact pea chloroplasts: II. Influence of electron transport regulators, uncouplers, ATPase and anion uptake inhibitors and protein binding reagents. Plant Physiol. 1988;86:384-89. https://doi.org/10.1104/pp.86.2.384
27. Shingles R, Roh MH, McCarty RE. Nitrite transport in chloroplast inner envelope vesicles. I. Direct measurement of proton-linked transport. Plant Physiol. 1996;112:1375-81. https://doi.org/10.1104/pp.112.3.1375
28. Sugiura M, Georgescu MN, Takahashi M. A nitrite transporter associated with nitrite uptake by higher plant chloroplasts. Plant Cell Physiol. 2007;48:1022–35. https://doi.org/10.1093/pcp/pcm073
29. Campbell WH. Nitrate reductase, structure, function and regulation: Bridging the gap between biochemistry and physiology. Annu Rev Plant Physiol Plant Mol Biol. 1999;50:277-303. https://doi.org/10.1146/annurev.arplant.50.1.277
30. Friemann A, Brinkmann K, Hachtel W. Sequence of a cdna encoding bi-specific NAD(P)H-nitrate reductase from the tree Betula pendula and identification of conserved protein regions. Mol Gen Genomics. 1991;227:97-105. http://doi..org/10.1007/bf00260713
31. Zhou J, Kleinhofs A. Molecular evolution of nitrate reductase genes. J Mol Evol. 1996;42:432-42. https://doi.org/10.1007/BF02498637
32. Schondorf T, Hachtel W. The choice of reducing substrate is altered by replacement of an alanine by proline in the FAD domain of a bispecific NADH(P)H-nitrate reductase from birch. Plant Physiol. 1995;108:203-10. https://doi.org/10.1104/pp.108.1.203
33. Campbell WH. Molecular control of nitrate reductase and other enzymes involved in nitrate assimilation. In: Foyer CH, Noctor G, editors. Photosynthetic nitrogen assimilation and associated carbon and respiratory metabolism. Dordecht: Kluwer Academic Publishers; 2002. p. 35-48. https://doi.org/10.1007/0-306-48138-3_3
34. Campbell WH. Nitrate reductase biochemistry comes of age. Plant Physiol. 1996;111:355-61. https://doi.org/10.1104/pp.111.2.355
35. Schwarz G, Mendel RR. Molybdenum cofactor biosynthesis and molybdenum enzymes. Annu Rev Plant Biol. 2006;57:623-47. https://doi.org/10.1146/annurev.arplant.57.032905.105437
36. Kamachi K, Amemiya Y, Ogura N, Nakagawa H. Immuno-gold localization of nitrate reductase in spinach (Spinacea oleracea) leaves. Plant Cell Physiol. 1987;28:333-38. https://doi.org/10.1093/oxfordjournals.pcp.a077300
37. Solomonson LP, Barber MJ. Assimilatory nitrate reductase: functional properties and regulation. Annu Rev Plant Physiol Plant Mol Biol. 1990;41:225-53. https://doi.org/10.1146/annurev.pp.41.060190.001301
38. Yamasaki H, Sakihama Y. Simultaneous production of nitric oxide and peroxynitrite by nitrate reductase: in vitro evidence for the NR-dependent formation of active nitrogen species. FEBS Lett. 2000;468:89-92. http://doi.org/10.1016/s0014-5793(00)01203-5
39. Chamizo-Ampudia A, Sanz-Luque E, Llamas A, Galvan A, Fernandez E. Nitrate Reductase Regulates Plant Nitric Oxide Homeostasis. Trends Plant Sci. 2017;22:163–74. DOI:10.1016/j.tplants.2016.12.001
40. Rockel P, Strube F, Rockel A, Wildt J, Kaiser WM. Regulation of nitric oxide (NO) production by plant nitrate reductase in vivo and in vitro. J Exp Bot. 2002;53:103-10. https://doi.org/10.1093/jexbot/53.366.103
41. Stöhr C, Strube P, Marx G, Ullrich, WR, Rockel P. A plasma-membrane-bound enzyme of tobacco or roots catalyses the formation of nitric oxide from nitrite. Planta. 2001;212:835-41. https://doi.org/10.1007/s004250000447
42. Prochazkova D, Haisel D, Pavlikova D. Nitric oxide biosynthesis in plants—the short overview. Plant Soil Environ. 2014;60:129–34. https://doi.org/10.17221/901/2013-PSE
43. Oaks A, Hirel B. Nitrogen Metabolism in roots. Annu Rev Plant Physiol. 1985;36:345-65. https://doi.org/10.1146/annurev.pp.36.060185.002021
44. Schuster C, Mohr H. Photooxidative damage to plastids affects the abundance of nitrate reductase mRNA in mustard cotyledons. Planta. 1990;181:125-28. https://doi.org/10.1007/BF00202334
45. Schuster C, Mohr H. Appearance of nitrite reductase mRNA in mustard seedling cotyledons is regulated by phytochrome. Planta. 1990;181:327-34. https://doi.org/10.1007/BF00195884
46. Yoneyama T, Suzuki A. Exploration of nitrate-to-glutamate assimilation in non-photosynthetic roots of higher plants by studies of (15)N-tracing, enzymes involved, reductant supply, and nitrate signaling: A review and synthesis. Plant Physiol Biochem. 2019;136:245–54. https://doi.org/10.1016/j.plaphy.2018.12.011
47. Bowsher CG, Hucklesby DP, Emes MJ. Induction of ferredoxin-NADP+oxidoreductase and ferredoxin synthesis in pea root plastids during nitrate assimilation. Plant J. 1993;3:463-67. https://doi.org/10.1111/j.1365-313X.1993.tb00166.x
48. Hase T, Schürmann P, Knaff DB. The interaction of ferredoxin with ferredoxin-dependent enzymes. In: Golbeck J, editor. Photosystem 1. Dordrecht, The Netherlands: Springer; 2006. p. 477–98. https://doi.org/10.1007/978-1-4020-4256-0_28
49. Fariduddin Q, Varshney P, Ali A. Perspective of nitrate assimilation and bioremediation in Spirulina platensis (a non-nitrogen fixing cyanobacterium): An overview. J Env Biol. 2018;39:547-57. http://doi.org/10.22438/jeb/39/5/MS-172
50. Sivasankar S, Rothstein S, Oaks A. Regulation of the accumulation and reduction of nitrate by nitrogen and carbon metabolites in maize seedlings. Plant Physiol. 1997;114:583-89. https://doi.org/10.1104/pp.114.2.583.
51. Maia LB, Moura JGJ. How biology handles nitrite. Chem. Rev. 2014;114:5273-357. https://doi.org/10.1021/cr400518y
52. Duncanson E, Gilkes AF, Kirk DW, Sheman A, Wray JL. Niri, a conditional-lethal mutant in barley causing a defect in nitrite reduction. Mol Gen Genet. 1993;236:275-82. https://doi.org/10.1007/BF00277123
53. Kishorekumar R, Bulle M, Wany A, Gupta KJ. An Overview of Important Enzymes Involved in Nitrogen Assimilation of Plants. In: Gupta K. Editor. Nitrogen Metabolism in Plants. Methods in Molecular Biology, 2020; vol 2057. New York Humana. https://doi.org/10.1007/978-1-4939-9790-9_1
54. Coruzzi GM. Primary N-assimilation into Amino Acids in Arabidopsis. The Arabidopsis Book. 2003;2:e0010. http://doi.org10.1199/tab.0010
55. Melo-Oliveira R, Cinha-Oliveira I, Coruzzi GM. Arabidopsis mutant analysis and gene regulation define a non-redundant role for glutamate dehydrogenase in nitrogen assimilation. Proc Natl Acad Sci USA. 1996;96:4718-23. https://doi.org/10.1073/pnas.93.10.4718
56. Anjana, Umar S, Iqbal M. Nitrate accumulation in plants, factors affecting the process, and human health implications. A review. Agron Sustain Dev. 2007;27:45-57. https://doi.org/10.1051/agro:2006021
57. Secheley KA, Yamata T, Oaks A. Compartmentation of nitrogen assimilation in higher plants. Int Rev Cyt. 1992;134:85-163. https://doi.org/10.1016/S0074-7696(08)62028-8
58. Cren M, Hirel B. Glutamine synthetase in higher plants: Regulation of gene and protein expression from the organ to the cell. Plant Cell Physiol. 1999;40:1187-93. https://doi.org/10.1093/oxfordjournals.pcp.a029506
59. Inokuchi R, Kuma K, Miyata T, Okada M. Nitrogen-assimilating enzymes in land plants and algae: phylogenic and physiological perspectives. Physiol Plant. 2002;116:1-11. https://doi.org/10.1034/j.1399-3054.2002.1160101.x
60. Lam HM, Coschigano KT, Oliveira IC, Melo-Oliveira R, Coruzzi GM. The molecular genetics of nitrogen assimilation into amino acids in higher plants. Annu Rev Plant Physiol Plant Mol Biol. 1996;47:569-93. https://doi.org/10.1146/annurev.arplant.47.1.569
61. Masclaux-Daubresse C, Daniel-Vedele F, Dechorgnat J, Chardon F, Gaufichon L, Suzuki A., Nitrogen uptake, assimilation and remobilization in plants: challenges for sustainable and productive agriculture, Annals Bot. 2010;105:1141–57. https://doi.org/10.1093/aob/mcq028
62. Suzuki A, Knaff DB. Glutamate synthase: structural, mechanistic and regulatory properties, and role in the amino acid metabolism. Photosynth Res. 2005;83:191-217. https://doi.org/10.1007/s11120-004-3478-0
63. Temple SJ, Vance CP, Gantt JS. Glutamate synthase and nitrogen assimilation. Trends Plant Sci. 1998;3:51-56. https://doi.org/10.1016/S1360-1385(97)01159-X
64. Forde B, Lea P. Glutamate in plants: Metabolism, regulation, and signalling. J Exp Bot. 2007; 58:2339-58. https://doi.org/10.1093/jxb/erm121
65. Hayakawa T, Nakamura T, Hattori F, Mae T, Ojima K, Yamaya T. Cellular localization of NADH-dependent glutamate synthase protein in vascular bundles of unexpanded leaf blades and young grains of rice plants. Planta. 1994;193:455-60. https://doi.org/10.1007/BF00201826
66. Coshigano KT, Melo-Oliveira R, Lim J, Coruzzi GM. Arabidopsis gls mutants and distinct Fd-GOGAT genes: implication for photorespiration and primary nitrogen assimilation. Plant Cell. 1998;10:741-52. https://doi.org/10.1105/tpc.10.5.741
67. Hirasawa M, Hurley JK, Salamon Z, Tollin G, Knaff DB. Oxidation-reduction and transient kinetics of ferredoxin dependent glutamate synthase. Arch Biochem Biophys. 1996; 330: 209-15. https://doi.org/10.1006/abbi.1996.0244
68. Sakakibara H, Kawabata S, Hase T, Sugiyama T. Differential effect of nitrate and light on the expression of glutamine synthetase and ferredoxin-dependent glutamate synthase in maize. Plant Cell Physiol. 1992;33:1193-98. https://doi.org/10.1093/oxfordjournals.pcp.a078373
69. Migge A, Carrayol E, Hirel B, Lohmann M, Meya G, Becker TW. Influence of UV-A or UV-B light and of the nitrogen source on the induction of ferredoxin-dependent glutamate synthase in etiolated tomato cotelydons. Plant Physiol Biochem. 1998;36:789-97. https://doi.org/10.1016/S0981-9428(99)80015-1
70. Hecht U, Oelmuller R, Schmidt S, Mohr H. Action of light, nitrate and ammonium on the levels of NADH- and ferredoxin-dependent glutamate synthase in the cotyledons of mustard seedlings. Planta. 1988;175:130-38. https://doi.org/10.1007/BF00402890
71. Yamaya T, Hayakawa T, Tanasawa K, Kamachi K, Mae T, Ojima K. Tissue distribution of glutamate synthase and glutamine synthetase in rice leaves. Occurrence of NADH-dependent glutamate synthase protein and activity in the unexpanded non-green leaf blades. Plant Physiol. 1992;100:1427-32. https://doi.org/10.1104/pp.100.3.1427
72. Kubik-Dobasz G. The activity of NADH, NADPH and ferredoxin-dependent glutamate synthase in the plastids and cytosol of Pisum arvense L. root cells. Acta Societatis Botanicorum Poloniae. 1989;58:253–62. https://doi.org/10.5586/asbp.1989.021
73. Rus-Alvarez A, Guerrier G. Proline metabolic pathways in calli from Lycopersicum esculentum and L. Pennellii under salt stress. Biol Plant (Prague). 1994;36:277-84. https://doi.org/10.1007/BF02921101
74. Foyer CH, Ferrario S. Modulation of carbon and nitrogen metabolism in transgenic plants with a view to improved biomass production. Biochem Soc Transac. 1994;22:909-15. https://doi.org/10.1042/bst0220909
75. Oliveira IC, Brenner E, Chiu J, Hsieh M-H, Kouranov A, Lam H-M, Shin MJ, Coruzzi G. Metabolite and light regulation of metabolism in plants: lessons from the study of a single biochemical pathway. Braz J Med Biol Res. 2001;34:567-75. http://dx.doi.org/10.1590/S0100-879X2001000500003
76. Kant S, Seneweera S, Rodin J, Materne M, Burch D, Rothstein SJ, Spangenberg G. Improving yield potential in crops under elevated CO2: integrating the photosynthetic and nitrogen utilization efficiencies. Front Plant Sci. 2012;3:162. https://doi.org/10.3389/fpls.2012.00162
77. Kaiser WM, Kandlbinder A, Stoimenova M, Glaab J. Discrepancy between nitrate reduction rates in intact leaves and nitrate reductase activity in leaf extracts: what limits nitrate reduction in situ? Planta. 2000;210:801–07. https://doi.org/10.1007/s004250050682
78. Xu G, Fan X, Miller AJ. Plant nitrogen assimilation and use efficiency. Annu Rev Plant Biol. 2012;63:153–82. https://doi.org/10.1146/annurev-arplant-042811-105532
79. Foyer C, Ferario-Mery S, Noctor G. Interactions between carbon and nitrogen metabolism. In: Lea PJ, Morot-Gaudry JF, editors. Plant nitrogen. Berlin: Springer Verlag; 2001. p. 237–54. https://doi.org/10.1007/978-3-662-04064-5_9
80. Li H, Liang Z, Ding G, Shi L, Xu F, Cai H. A Natural Light/Dark Cycle Regulation of Carbon-Nitrogen Metabolism and Gene Expression in Rice Shoots. Front Plant Sci. 2016;7:1318. https://doi.org/10.3389/fpls.2016.01318
81. Scheible WR, Gonzales-Fontes A, Morcuende R, Lauerer M, Geiger M, Glaab J, Schulze E-D, Stitt M. Tobacco mutants with a decreased number of functional nia-genes compensate by modifying the diurnal regulation transcription, post-translational modification and turnover of nitrate reductase. Planta. 1997;203:305–19. https://doi.org/10.1007/s004250050196
82. Lewis E, Noctor G, Causton D, Foyer CH. Regulation of assimilate partitioning in leaves. Aust J Plant Physiol. 2000; 27: 507-17. https://doi.org/10.1071/PP99177
83. Aslam M, Huffaker RC, Rains DW, Rao KP. Influence of light and ambient carbon dioxide concentration on nitrate assimilation by intact barley seedlings. Plant Physiol. 1979;63:1205-09. https://doi.org/10.1104/pp.63.6.1205
84. Nunes-Nesi A, Fernie AR, Stitt M. Metabolic andsignaling aspects underpinning the regulation of plant carbon nitrogen interactions. Mol Plant. 2010;3:973–96. https://doi.org/10.1093/mp/ssq049
85. Emes MJ, Neuhaus HE. Metabolism and transport in non-photosynthetic plastids. J Exp Bot. 1997;48:1995-2005. https://doi.org/10.1093/jxb/48.12.1995
86. Banks FM, Driscoll SP, Parry MAJ, Lawlor DW, Knight JS, Gray JC, et al. Decrease in phosphoribulokinase activity by antisense RNA in transgenic tobacco: relationship between photosynthesis, growth, and allocation at contrasting nitrogen supplies. Plant Physiol. 1999;119:1125-36. https://doi.org/10.1104/pp.119.3.1125
87. Morcuende R, Krapp A, Hurry V, Stitt M. Sucrose feeding leads to increased rates of nitrate assimilation, increased rates of oxoglutarate synthesis, and increased synthesis of a wide spectrum of amino acids in tobacco leaves. Planta. 1998;206:394–409. https://doi.org/10.1007/s004250050415
88. Amory AM, Vanlerberghe GC, Turpin DH. Demonstration of both a photosynthetic and nonphotosynthetic CO2 requirement for NH4+ assimilation in the green alga Selenastrumminutum. Plant Physiol. 1991;95:192-96. https://doi.org/10.1104/pp.95.1.192
89. Elrifi IR, Holmes JJ, Weger HG, Mayo WP, Turpin DH. Rubp limitation of photosynthetic carbon fixation during NH3 assimilation. Interactions between photosynthesis, respiration, and ammonium assimilation in N-limited green algae. Plant Physiol. 1988;87:395-401.https://doi.org/10.1104/pp.87.2.395
90. Pace GM, Volk RJ, Jackson WA. Nitrate reduction in response to CO2-1imited photosynthesis. Relationship to carbohydrate supply and nitrate reductase activity in maize seedlings. Plant Physiol. 1990;92:286-92. https://doi.org/10.1104/pp.92.2.286
91. Galangau F, Daniel-VedBle F, Moureaux T, Dorbe MF, Leydecker MT, Caboche M. Expression of leaf nitrate reductase genes from tomato and tobacco in relation to light dark regimes and nitrate supply. Plant Physiol. 1988;88:383-88. https://doi.org/10.1104/pp.88.2.383
92. Stitt M, Krapp A. The interaction between elevated carbon dioxide and nitrogen nutrition: the physiological and molecular background. Plant Cell Environ. 1999;22:583–621. https://doi.org/10.1046/j.1365-3040.1999.00386.x
93. Rufty TW, Mackown CT, Volk RJ. Effects of altered carbohydrate availability on whole-plant assimilation of 15NO3-. Plant Physiol. 1989;89:457-63. https://doi.org/10.1104/pp.89.2.457
94. Le VQ, Foyer C, Champigny ML. Effect of light and NO3- on wheat leaf phosphoenolpyruvate carboxylase activity. Plant Physiol. 1991;97):1476-82. https://doi.org/10.1104/pp.97.4.1476
95. Vanlerberghe GC, Schuller KA, Smith RG, Feil R, Plaxton WC, Turpin, DH. Relationship between NH4+ assimilation rate and in vivo phosphoenolpyruvate carboxylase activity. Plant Physiol. 1990;94:284-290. https://doi.org/10.1104/pp.94.1.284
96. Krapp A. Plant nitrogen assimilation and its regulation: A complex puzzle with missing pieces. Curr Opin Plant Biol. 2015;25:115–22. https://doi.org/10.1016/j.pbi.2015.05.010
97. Lammerts van Bueren ET, Struik PC. Diverse concepts of breeding for nitrogen use efficiency. A review. Agron Sustain Dev. 2017;37:50. https://doi.org/10.1007/s13593-017-0457-3
98. Andrews M, Lea PJ, Raven JA, Lindsey K. Can genetic manipulation of plant nitrogen assimilation enzymes result in increased crop yield and greater N-use efficiency? An assessment. Annals App Biol. 2004;145:25-40. https://doi.org/10.1111/j.1744-7348.2004.tb00356.x
99. Hachiya T, Sakakibara H. Interactions between nitrate and ammonium in their uptake, allocation, assimilation, and signaling in plants. J Exp Bot. 2017;68:2501–12, https://doi.org/10.1093/jxb/erw449
100. Britto DT, Kronzucker HJ. NH4+ toxicity in higher plants: a critical review. J Plant Physiol. 2002;159:567-84.https://doi.org/10.1078/0176-1617-0774
Downloads
Published
01-04-2020
How to Cite
1.
Ali A. Nitrate assimilation pathway in higher plants: critical role in nitrogen signalling and utilization. Plant Sci. Today [Internet]. 2020 Apr. 1 [cited 2024 Apr. 26];7(2):182-9. Available from: https://horizonepublishing.com/journals/index.php/PST/article/view/637
Issue
Section
Review Articles
License
Copyright and Licence details of published articles
Authors who publish with this journal agree to the following terms:
- Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
- Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.
Open Access Policy
Plant Science Today is an open access journal. There is no registration required to read any article. All published articles are distributed under the terms of the Creative Commons Attribution License (CC Attribution 4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited (https://creativecommons.org/licenses/by/4.0/). Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).
