An insight: Impact of reduced Rubisco on plant physiology and biochemistry


Abstract views: 171 / PDF downloads: 73

Authors

  • CHIRAG MAHESHWARI ICAR-Central Institute of Agricultural Engineering, Bhopal 462 038, India
  • NITIN KUMAR GARG ICAR-Central Institute of Agricultural Engineering, Bhopal 462 038, India
  • MUZAFFAR HASSAN ICAR-Central Institute of Agricultural Engineering, Bhopal 462 038, India
  • ARUNA TYAGI ICAR-Central Institute of Agricultural Engineering, Bhopal 462 038, India

https://doi.org/10.56093/ijas.v91i1.110901

Keywords:

Photosynthesis, Plant growth, RubisCo

Abstract

Photosynthesis is a process of conversion of sunlight energy and atmospheric carbon to organic molecules with the help of a key and that is Ribulose-1,5-bisphosphate carboxylase/oxygenase. Ribulose-1,5-bisphosphate carboxylase/ oxygenase (RubisCo) is one of the most abundant proteins in the biosphere and a key enzyme in the global carbon cycle and its assimilation. RubisCo has been extensively studied regarding its structure, kinetics, evolution, etc. But still, many questions remain an illusion such as why plants maintain a large pool of RubisCo protein and its many isoforms; how the different isoforms coordinate their functions altogether and how does RubisCo affect photosynthetic rate, biomass allocation and vegetative growth of plants, although much research has been conducted in the recent past to answer these questions. In this review, different physiological, biochemical, and molecular studies aimed to reduce RubisCo in plants will be discussed to answer above mentioned questions and to better understand it's functioning.

Downloads

Download data is not yet available.

References

Alexandratos N and Bruinsma J. 2012. World agriculture towards 2030/2050: the 2012 revision.

Andersson I and Backlund A. 2008. Structure and function of Rubisco. Plant Physiology and Biochemistry 46(3): 275–91. DOI: https://doi.org/10.1016/j.plaphy.2008.01.001

Andrews T J and Lorimer G H. 1987. Rubisco: structure, mechanisms, and prospects for improvement. Photosynthesis, pp 131–218. Academic Press. DOI: https://doi.org/10.1016/B978-0-12-675410-0.50009-9

Andrews T J, Hudson G S, Mate C J, von Caemmerer S, Evans J R and Arvidsson Y B. 1995. Rubisco: the consequences of altering its expression and activation in transgenic plants. Journal of Experimental Botany 1293–1300. DOI: https://doi.org/10.1093/jxb/46.special_issue.1293

Chirag Maheshwari. 2020. ‘Impact of Ribulose-1,5-bisphosphate carboxylase/oxygenase (RUBISCO) knockdown on photosynthesis and growth characteristics of rice plants’. Ph D thesis, ICAR-Indian Agricultural Research Institute, New Delhi.

Dean C, Pichersky E and Dunsmuir P. 1989. Structure, evolution, and regulation of RbcS genes in higher plants. Annual Review of Plant Biology 40(1): 415–39. DOI: https://doi.org/10.1146/annurev.pp.40.060189.002215

Desa U. 2019. World Population Prospects 2019: Highlights. New York (US): United Nations Department for Economic and Social Affairs.

Evans J R. 1989. Photosynthesis and nitrogen relationships in leaves of C3 plants. Oecologia 78(1): 9–19. DOI: https://doi.org/10.1007/BF00377192

Farquhar G D and Von Caemmerer S. 1982. Modelling of photosynthetic response to environmental conditions. Physiological Plant Ecology II, pp 549–87. Springer, Berlin, Heidelberg. DOI: https://doi.org/10.1007/978-3-642-68150-9_17

Fichtner K, Quick W P, Schulze E D, Mooney H A, Rodermel S R, Bogorad L and Stitt M. 1993. Decreased ribulose-1, 5-bisphosphate carboxylase-oxygenase in transgenic tobacco transformed with “antisense” rbcS. Planta 190(1): 1–9. DOI: https://doi.org/10.1007/BF00195668

Furbank R T, Chitty J A, von Caemmerer S and Jenkins C L. 1996. Antisense RNA inhibition of RbcS gene expression reduces Rubisco level and photosynthesis in the C4 plant Flaveria bidentis. Plant Physiology 111(3): 725–34. DOI: https://doi.org/10.1104/pp.111.3.725

Hansen S, Hough E and Andersen K. 1999. Purification, crystallization and preliminary X-ray studies of two isoforms of Rubisco from Alcaligenes eutrophus. Acta Crystallographica Section D: Biological Crystallography 55(1): 310–13. DOI: https://doi.org/10.1107/S0907444998010257

Hudson G S, Evans J R, von Caemmerer S, Arvidsson Y B and Andrews T J. 1992. Reduction of ribulose-1, 5-bisphosphate carboxylase/oxygenase content by antisense RNA reduces photosynthesis in transgenic tobacco plants. Plant Physiology 98(1): 294–302. DOI: https://doi.org/10.1104/pp.98.1.294

Ishizuka M, Makino A, Suzuki Y and Mae T. 2004. Amount of Ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisco) Protein and levels of mRNAs of rbc S and rbc L in the leaves at different positions in transgenic rice plants with decreased content of Rubisco. Soil Science and Plant Nutrition 50(2): 233–39. DOI: https://doi.org/10.1080/00380768.2004.10408472

Izumi M, Tsunoda H, Suzuki Y, Makino A and Ishida H. 2012. RBCS1A and RBCS3B, two major members within the Arabidopsis RBCS multigene family, function to yield sufficient Rubisco content for leaf photosynthetic capacity. Journal of Experimental Botany 63(5): 2159–70. DOI: https://doi.org/10.1093/jxb/err434

Khan M I R, Palakolanu S R, Chopra P, Rajurkar A B, Gupta R, Iqbal N and Maheshwari C. (2020). Improving drought tolerance in rice: Ensuring food security through multi dimensional approaches. Physiologia Plantarum. DOI: https://doi.org/10.1111/ppl.13223

Kacser H and Burns J A. 1973. Rate control of biological processes. In Symp. Society of Experimental. Biology 27: 65–104.

Kanno K, Suzuki Y and Makino A. 2017. A small decrease in Rubisco content by individual suppression of RBCS genes leads to improvement of photosynthesis and greater biomass production in rice under conditions of elevated CO2. Plant and Cell Physiology 58(3): 635–42. DOI: https://doi.org/10.1093/pcp/pcx018

Lauerer M, Saftic D, Quick W P, Labate C, Fichtner K, Schulze E D and Stitt M. 1993. Decreased ribulose-1, 5-bisphosphate carboxylase-oxygenase in transgenic tobacco transformed with “antisense” rbcS. Planta 190(3): 332–45. DOI: https://doi.org/10.1007/BF00196962

Maheshwari, Chirag, Robert A Coe, Shanta Karki, Sarah Covshoff, Ronald Tapia, Aruna Tyagi, Julian M. Hibberd, Robert T Furbank, W Paul Quick and Hsiang-Chun Lin. 2020. Targeted knockdown of ribulose-1, 5-bisphosphate carboxylase-oxygenase in rice mesophyll cells impact on photosynthesis and growth. bioRxiv. DOI: https://doi.org/10.1101/2020.08.20.259382

Makino A, Nakano H, Mae T, Shimada T and Yamamoto N. 2000. Photosynthesis, plant growth, and N allocation in transgenic rice plants with decreased Rubisco under CO2 enrichment. Journal of Experimental Botany 51(suppl_1): 383–89. DOI: https://doi.org/10.1093/jexbot/51.suppl_1.383

Makino A, Shimada T, Takumi S, Kaneko K, Matsuoka M, Shimamoto K and Yamamoto N. 1997. Does decrease in ribulose-1, 5-bisphosphate carboxylase by antisense RbcS lead to a higher N-use efficiency of photosynthesis under conditions of saturating CO2 and light in rice plants? Plant Physiology 114(2): 483–91. DOI: https://doi.org/10.1104/pp.114.2.483

Masle J, Hudson G S and Badger M R. 1993. Effects of ambient CO2 concentration on growth and nitrogen use in tobacco (Nicotiana tabacum) plants transformed with an antisense gene to the small subunit of ribulose-1, 5-bisphosphate carboxylase/ oxygenase. Plant Physiology 103(4): 1075–88. DOI: https://doi.org/10.1104/pp.103.4.1075

Matt P, Krapp A, Haake V, Mock H P and Stitt M. 2002. Decreased Rubisco activity leads to dramatic changes of nitrate metabolism, amino acid metabolism, and the levels of phenylpropanoids and nicotine in tobacco antisense RBCS transformants. Plant Journal 30(6): 663–77. DOI: https://doi.org/10.1046/j.1365-313X.2002.01323.x

Morita K, Hatanaka T, Misoo S and Fukayama H. 2014. Unusual small subunit that is not expressed in photosynthetic cells alters the catalytic properties of Rubisco in rice. Plant Physiology 164(1): 69–79. DOI: https://doi.org/10.1104/pp.113.228015

Morse D, Salois P, Markovic P and Hastings J W. 1995. A nuclear-encoded form II RuBisCO in dinoflagellates. Science 268(5217): 1622–24. DOI: https://doi.org/10.1126/science.7777861

Parry M A J, Madgwick P J, Carvalho J F C and Andralojc P J. 2007. Prospects for increasing photosynthesis by overcoming the limitations of Rubisco. Journal of Agricultural Science 145(1): 31. DOI: https://doi.org/10.1017/S0021859606006666

Parry M A, Andralojc P J, Scales J C, Salvucci M E, Carmo-Silva A E, Alonso H and Whitney S M. 2013. Rubisco activity and regulation as targets for crop improvement. Journal of Experimental Botany 64(3): 717–30. DOI: https://doi.org/10.1093/jxb/ers336

Pearce F G and Andrews T J. 2003. The relationship between side reactions and slow inhibition of ribulose-bisphosphate carboxylase revealed by a loop 6 mutant of the tobacco enzyme. Journal of Biological Chemistry 278(35): 32526–36. DOI: https://doi.org/10.1074/jbc.M305493200

Quick W P, Schurr U, Fichtner K, Schulze E D, Rodermel S R, Bogorad L and Stitt M. 1991. The impact of decreased Rubisco on photosynthesis, growth, allocation, and storage in tobacco plants which have been transformed with antisense rbcS. Plant Journal 1(1): 51–58. DOI: https://doi.org/10.1111/j.1365-313X.1991.00051.x

Quick W P, Fichtner K, Wendler R, Schulze E D, Rodermel S R, Bogorad L and Stitt M. 1992. Decreased ribulose-1,5- bisphosphate carboxylase-oxygenase in transgenic tobacco transformed with “antisense” rbcS. IV. Impact on photosynthesis in conditions of altered nitrogen supply. Planta 188: 522–31. DOI: https://doi.org/10.1007/BF00197044

Ren L, Salnikow J and Vater J. 1991. Multiple forms of the small subunit of ribulose-1, 5-bisphosphate carboxylase/oxygenase in maize, and spinach. Plant Science 74(1): 1–6. DOI: https://doi.org/10.1016/0168-9452(91)90249-8

Rodermel S R, Abbott M S and Bogorad L. 1988. Nuclear-organelle interactions: nuclear antisense gene inhibits ribulose bisphosphate carboxylase enzyme levels in transformed tobacco plants. Cell 55(4): 673–81. DOI: https://doi.org/10.1016/0092-8674(88)90226-7

Sage R F. 1990. A model describing the regulation of ribulose-1, 5-bisphosphate carboxylase, electron transport, and triose phosphate use in response to light intensity and CO2 in C3 plants. Plant Physiology 94(4): 1728–34. DOI: https://doi.org/10.1104/pp.94.4.1728

Sharkey T D. 1989. Evaluating the role of Rubisco regulation in photosynthesis of C3 plants. Philosophical Transactions of the Royal Society of London. B, Biological Sciences 323(1216): 435–48. DOI: https://doi.org/10.1098/rstb.1989.0022

Simkin A J, López-Calcagno P E and Raines C A. 2019. Feeding the world: improving photosynthetic efficiency for sustainable crop production. Journal of Experimental Botany 70(4): 1119–40. DOI: https://doi.org/10.1093/jxb/ery445

Spreitzer R J. 2003. Role of the small subunit in ribulose-1, 5-bisphosphate carboxylase/oxygenase. Archives of Biochemistry and biophysics 414(2): 141–49. DOI: https://doi.org/10.1016/S0003-9861(03)00171-1

Stec B. 2012. Structural mechanism of RuBisCO activation by carbamylation of the active site lysine. Proceedings of the National Academy of Sciences 109(46): 18785-90. DOI: https://doi.org/10.1073/pnas.1210754109

Stilt M, Quick W P, Schurr U, Schulze E D, Rodermel S R and Bogorad, L. 1991. Decreased ribulose-l, 5-bisphosphate carboxylase-oxygenase in transgenic tobacco transformed with ‘antisense’ rbcS. I1. Flux-control coefficients for photosynthesis in varying light, CO2, and air humidity. Planta 183: 555–66. DOI: https://doi.org/10.1007/BF00194277

Stitt M and Schulze D. 1994. Does Rubisco control the rate of photosynthesis and plant growth? An exercise in molecular ecophysiology. Plant, Cell and Environment 17(5): 465–87. DOI: https://doi.org/10.1111/j.1365-3040.1994.tb00144.x

Suzuki Y, Miyamoto T, Yoshizawa R, Mae T and Makino A. 2009. Rubisco content and photosynthesis of leaves at different positions in transgenic rice with an overexpression of RBCS. Plant, Cell and Environment 32(4): 417–27. DOI: https://doi.org/10.1111/j.1365-3040.2009.01937.x

Tyagi A and Chandra A. 2006. Isolation of stress responsive Psb A gene from rice (Oryza sativa L.) using differential display.

Tabita F R, Hanson T E, Li H, Satagopan S, Singh J and Chan S. 2007. Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs. Microbiol. Mol. Biol. Rev 71(4): 576–99. DOI: https://doi.org/10.1128/MMBR.00015-07

Vitlin Gruber A and Feiz L. 2018. Rubisco assembly in the chloroplast. Frontiers in Molecular Biosciences 5: 24. DOI: https://doi.org/10.3389/fmolb.2018.00024

Von Caemmerer S, Evans J R, Hudson G S and Andrews T J. 1994. The kinetics of ribulose-1, 5-bisphosphate carboxylase/ oxygenase in vivo inferred from measurements of photosynthesis in leaves of transgenic tobacco. Planta 195(1): 88–97. DOI: https://doi.org/10.1007/BF00206296

Whitney S M, Houtz R L and Alonso H. 2011. Advancing our understanding and capacity to engineer nature’s CO2- sequestering enzyme, Rubisco. Plant Physiology 155(1): 27–35. DOI: https://doi.org/10.1104/pp.110.164814

Downloads

Submitted

2021-03-01

Published

2021-03-02

Issue

Section

Review Article

How to Cite

MAHESHWARI, C., GARG, N. K., HASSAN, M., & TYAGI, A. (2021). An insight: Impact of reduced Rubisco on plant physiology and biochemistry. The Indian Journal of Agricultural Sciences, 91(1), 16–20. https://doi.org/10.56093/ijas.v91i1.110901
Citation