Abstract
Rubisco activase functions to promote and maintain the catalytic activity of Rubisco. Studies with the activase-lacking Arabidopsis rca mutant (Salvucci et al. Photosynth Res 7:193–201, 1985; Salvucci et al. Plant Physiol 80:655–659, 1986), antisense activase tobacco, Arabidopsis and Flaveria bidentis plants (Mate et al. Plant Physiol 102:1119–1128, 1993; Eckardt et al. Plant Physiol 113:575–586, 1997; von Caemmerer et al. Plant Physiol 137:747–755, 2005) have shown that photosynthesis at atmospheric levels of CO2 is severely impaired when plants lack activase because Rubisco becomes sequestered in an inactive form. Activase protein has been detected in all plant species, including C3 and C4 plants and green algae (Salvucci et al. Plant Physiol 84:930–936, 1987). Rubisco activase is essential in all these photosynthetic organisms for photosynthesis and plant growth. The physiological importance of Rubisco activase is reinforced by recent studies indicating that it plays a role in the response of photosynthesis to temperature. In this chapter, we describe how to extract and quantify Rubisco activase content in leaf.
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References
Salvucci, M.E., Portis, A.R. Jr., and Ogren, W.L. (1985) A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase/oxygenase activation in vivo. Photosynth Res 7, 193–201.
Salvucci, M.E., Portis, A.R. Jr., and Orgen, W.L. (1986) Light and CO2 response of ribulose-1,5-bisphosphate carboxylase/oxygenase activation in Arabidopsis leaves. Plant Physiol 80, 655–659.
Mate, C.J., Hudson, G.S., von Caemmerer, S., Evans, J.R., and Andrews, T.J. (1993) Reduction of ribulose-bisphosphate carboxylase activase levels in tobacco (Nicotiana tabacum) by antisense RNA reduces ribulose bisphosphate carboxylase carbamylation and impairs photosynthesis. Plant Physiol 102, 1119–1128.
Eckardt, N.A., Snyder, G.W., Portis, A.R. Jr., and Ogren, W.L. (1997) Growth and photosynthesis under high and low irradiance of Arabidopsis thaliana antisense mutants with reduced ribulose-1,5-bisphosphate carboxylase/oxygenase activase content. Plant Physiol 113, 575–586.
von Caemmerer, S., Hendrickson, L., Quinn, V., Vella, N., Millgate, A.G., and Furbank, R.T. (2005) Reductions of Rubisco activase by antisense RNA in the C4 plant Flaveria bidentis reduces Rubisco carbamylation and leaf photosynthesis. Plant Physiol 137, 747–755.
Salvucci, M.E., Werneke, J.M., Portis, A.R. Jr., and Ogren, W.L. (1987) Purification and species distribution of Rubisco activase. Plant Physiol 84, 930–936.
Andrews, T.J. and Lorimer, G.H. (1987) Rubisco: Structure, mechanisms, and prospects for improvement, in The Biochemistry of Plants: A Comprehensive Treatise, Vol. 10, Photosynthesis (Hatch, M.D. and Boardman, N.K., eds.), Academic Press, New York, pp. 131–218.
Portis, A.R. Jr. (2003) Rubisco activase: Rubisco’s catalytic chaperone. Photosynth Res 75, 11–27.
Salvucci, M.E. and Crafts-Brandner, S.J. (2004) Inhibition of photosynthesis by heat stress: the activation state of Rubisco as a limiting factor in photosynthesis. Physiol Plant 120, 179–186.
Parry, M.A.J., Keys, A.J., Madgwick, P.J., Carmo-Silva, A.E., and Andralojc, P.J. (2008) Rubisco regulation: a role for inhibitors. J Exp Bot 59, 1569–1580
Andrews, T.J. (1996) The bait in the Rubisco mousetrap. Nat Struct Biol 3, 3–7.
Spreitzer, R.J. and Salvucci, M.E. (2002) Rubisco: interactions, associations and the possibilities of a better enzyme. Annu Rev Plant Biol 53, 449–475.
Rundle, S.J. and Zielinski, R.E. (1991) Organization and expression of two tandomly oriented genes encoding ribulosebisphosphate carboxylase/oxygenase activase in barley. J Biol Chem 266, 4677–4685.
Salvucci, M.E., van de Loo, F.J., and Stecher, D.S. (2003) Two isoforms of Rubisco activase in cotton, the products of separate genes not alternative splicing. Planta 216, 736–744.
Werneke, J.M., Zielinski, R.E., and Ogren, W.L. (1988) Structure and expression of spinach leaf cDNA-encoding ribulosebisphosphate carboxylase oxygenase activase. Proc Natl Acad Sci U S A 85, 787–791.
Zhang, N. and Portis, A.R. Jr. (1999) Mechanism of light regulation of Rubisco: a specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f. Proc Natl Acad Sci U S A 96, 9438–9443.
Qian, J. and Rodermel, S.R. (1993) Ribulose-1,5-bisphosphate carboxylase/oxygenase activase cDNAs from Nicotiana tabacum. Plant Physiol 102, 683–684.
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Yamori, W., von Caemmerer, S. (2011). Quantification of Rubisco Activase Content in Leaf Extracts. In: Carpentier, R. (eds) Photosynthesis Research Protocols. Methods in Molecular Biology, vol 684. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60761-925-3_30
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