Rubisco catalytic properties of wild and domesticated relatives provide scope for improving wheat photosynthesis

Prins, Anneke, Orr, Douglas J., Andralojc, P. John, Reynolds, Matthew P., Carmo-Silva, Elizabete and Parry, Martin A. J. (2016) Rubisco catalytic properties of wild and domesticated relatives provide scope for improving wheat photosynthesis. Journal of Experimental Botany, 67 (6). pp. 1827-1838. ISSN 0022-0957 (doi:10.1093/jxb/erv574)

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Abstract

Rubisco is a major target for improving crop photosynthesis and yield, yet natural diversity in catalytic properties of this enzyme is poorly understood. Rubisco from 25 genotypes of the Triticeae tribe, including wild relatives of bread wheat (Triticum aestivum), were surveyed to identify superior enzymes for improving photosynthesis in this crop. In vitro Rubisco carboxylation velocity (V c), Michaelis–Menten constants for CO2 (K c) and O2 (K o) and specificity factor (S c/o) were measured at 25 and 35 °C. V c and K c correlated positively, while V c and S c/o were inversely related. Rubisco large subunit genes (rbcL) were sequenced, and predicted corresponding amino acid differences analysed in relation to the corresponding catalytic properties. The effect of replacing native wheat Rubisco with counterparts from closely related species was analysed by modelling the response of photosynthesis to varying CO2 concentrations. The model predicted that two Rubisco enzymes would increase photosynthetic performance at 25 °C while only one of these also increased photosynthesis at 35 °C. Thus, under otherwise identical conditions, catalytic variation in the Rubiscos analysed is predicted to improve photosynthetic rates at physiological CO2 concentrations. Naturally occurring Rubiscos with superior properties amongst the Triticeae tribe can be exploited to improve wheat photosynthesis and crop productivity.

Item Type: Article
Additional Information: First published online: January 21, 2016
Research Areas: A. > School of Science and Technology
Item ID: 18831
Notes on copyright: © The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
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Depositing User: Anneke Prins
Date Deposited: 08 Feb 2016 12:04
Last Modified: 04 Apr 2019 16:29
URI: https://eprints.mdx.ac.uk/id/eprint/18831

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