Kapralov, MV, Smith, JA and Filatov, DA (2012) Rubisco evolution in C₄ eudicots: an analysis of Amaranthaceae sensu lato. PLoS One, 7 (12). ISSN 1932-6203
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Abstract
BACKGROUND: Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalyses the key reaction in the photosynthetic assimilation of CO₂. In C₄ plants CO₂ is supplied to Rubisco by an auxiliary CO₂-concentrating pathway that helps to maximize the carboxylase activity of the enzyme while suppressing its oxygenase activity. As a consequence, C₄ Rubisco exhibits a higher maximum velocity but lower substrate specificity compared with the C₃ enzyme. Specific amino-acids in Rubisco are associated with C₄ photosynthesis in monocots, but it is not known whether selection has acted on Rubisco in a similar way in eudicots. METHODOLOGY/PRINCIPAL FINDINGS: We investigated Rubisco evolution in Amaranthaceae sensu lato (including Chenopodiaceae), the third-largest family of C₄ plants, using phylogeny-based maximum likelihood and Bayesian methods to detect Darwinian selection on the chloroplast rbcL gene in a sample of 179 species. Two Rubisco residues, 281 and 309, were found to be under positive selection in C₄ Amaranthaceae with multiple parallel replacements of alanine by serine at position 281 and methionine by isoleucine at position 309. Remarkably, both amino-acids have been detected in other C₄ plant groups, such as C₄ monocots, illustrating a striking parallelism in molecular evolution. CONCLUSIONS/SIGNIFICANCE: Our findings illustrate how simple genetic changes can contribute to the evolution of photosynthesis and strengthen the hypothesis that parallel amino-acid replacements are associated with adaptive changes in Rubisco.
Item Type: | Article |
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Uncontrolled Keywords: | MD Multidisciplinary |
Subjects: | Q Science > QH Natural history > QH301 Biology Q Science > QH Natural history > QH426 Genetics |
Divisions: | Natural Sciences & Psychology (closed 31 Aug 19) |
Publisher: | Public Library of Science |
Related URLs: | |
Date Deposited: | 20 May 2015 14:53 |
Last Modified: | 04 Sep 2021 14:22 |
DOI or ID number: | 10.1371/journal.pone.0052974 |
URI: | https://researchonline.ljmu.ac.uk/id/eprint/1115 |
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