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Lookup NU author(s): Dr Maxim KapralovORCiD
This is the authors' accepted manuscript of an article that has been published in its final definitive form by Nature Publishing Group , 2016.
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Enhancing the catalytic properties of the CO2-fixing enzyme Rubisco is a target for improving agricultural crop productivity. Here, we reveal extensive diversity in the kinetic response between 10 and 37 °C by Rubisco from C3 and C4 species within the grass tribe Paniceae. The CO2 fixation rate (k c cat kcatc ) for Rubisco from the C4 grasses with nicotinamide adenine dinucleotide (NAD) phosphate malic enzyme (NADP-ME) and phosphoenolpyruvate carboxykinase (PCK) photosynthetic pathways was twofold greater than the k c cat kcatc of Rubisco from NAD-ME species across all temperatures. The declining response of CO2/O2 specificity with increasing temperature was less pronounced for PCK and NADP-ME Rubisco, which would be advantageous in warmer climates relative to the NAD-ME grasses. Modelled variation in the temperature kinetics of Paniceae C3 Rubisco and PCK Rubisco differentially stimulated C3 photosynthesis relative to tobacco above and below 25 °C under current and elevated CO2. Amino acid substitutions in the large subunit that could account for the catalytic variation among Paniceae Rubisco are identified; however, incompatibilities with Paniceae Rubisco biogenesis in tobacco hindered their mutagenic testing by chloroplast transformation. Circumventing these bioengineering limitations is critical to tailoring the properties of crop Rubisco to suit future climates.
Author(s): Sharwood RE, Ghannoum O, Kapralov MV, Gunn LH, Whitney SM
Publication type: Article
Publication status: Published
Journal: Nature Plants
Online publication date: 28/11/2016
Acceptance date: 27/10/2016
Date deposited: 02/11/2017
ISSN (print): 2055-026X
ISSN (electronic): 2055-0278
Publisher: Nature Publishing Group
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