ArticleJournal of experimental botany2014
Positive selection of Kranz and non-Kranz C4 phosphoenolpyruvate carboxylase amino acids in Suaedoideae (Chenopodiaceae).
Article in Journal of experimental botany, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Protoplast isolation and transient gene expression in Suaeda aralocaspica, a halophyte with single-cell CPlant methods · 2026Article
- Article
- Testing the kinetic tradeoff between bicarbonate versus phosphoenolpyruvate affinity and glucose-6 phosphate response of phosphoenolpyruvate carboxylase from two CPhotosynthesis research · 2025Article
- Leaf transcriptomes from C3, C3-C4 intermediate, and C4Neurachne species give insights into C4 photosynthesis evolution.Plant physiology · 2024Article
- Lighting the way: Compelling open questions in photosynthesis research.The Plant cell · 2024Article
- Multiple highly expressed phosphoenolpyruvate carboxylase genes have divergent enzyme kinetic properties in two C4 grasses.Annals of botany · 2023Article
- A Machine Learning Framework Identifies Plastid-Encoded Proteins Harboring C3 and C4 Distinguishing Sequence Information.Genome biology and evolution · 2023Article
- Differential timing of gene expression and recruitment in independent origins of CAM in the Agavoideae (Asparagaceae).The New phytologist · 2022Article
- Genome-Wide Identification and Analysis of the Phosphoenolpyruvate Carboxylase Gene Family inFrontiers in plant science · 2021Article
- Molecular Cloning of Novel-Type PhosphoPlants (Basel, Switzerland) · 2020Article
- Identification and evolution of CBMC plant biology · 2020Article
- Evolutionary Convergence of CFrontiers in plant science · 2020Article
- The genetics of convergent evolution: insights from plant photosynthesis.Nature reviews. Genetics · 2019Review
- A single serine to alanine substitution decreases bicarbonate affinity of phosphoenolpyruvate carboxylase in C4Flaveria trinervia.Journal of experimental botany · 2019Article
- EfficientFrontiers in plant science · 2019Article
- Identification of the allosteric site for neutral amino acids in the maize CThe Journal of biological chemistry · 2018Article
- Article
- Kranz and single-cell forms of C4 plants in the subfamily Suaedoideae show kinetic C4 convergence for PEPC and Rubisco with divergent amino acid substitutions.Journal of experimental botany · 2015Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
In subfamily Suaedoideae, four independent gains of C4 photosynthesis are proposed, which includes two parallel origins of Kranz anatomy (sections Salsina and Schoberia) and two independent origins of single-cell C4 anatomy (Bienertia and Suaeda aralocaspica). Additional phylogenetic support for this hypothesis was generated from sequence data of the C-terminal portion of the phosphoenolpyruvate carboxylase (PEPC) gene used in C4 photosynthesis (ppc-1) in combination with previous sequence data. ppc-1 sequence was generated for 20 species in Suaedoideae and two outgroup Salsola species that included all types of C4 anatomies as well as two types of C3 anatomies. A branch-site test for positively selected codons was performed using the software package PAML. From labelling of the four branches where C4 is hypothesized to have developed (foreground branches), residue 733 (maize numbering) was identified to be under positive selection with a posterior probability >0.99 and residue 868 at the >0.95 interval using Bayes empirical Bayes (BEB). When labelling all the branches within C4 clades, the branch-site test identified 13 codons to be under selection with a posterior probability >0.95 by BEB; this is discussed considering current information on functional residues. The signature C4 substitution of an alanine for a serine at position 780 in the C-terminal end (which is considered a major determinant of affinity for PEP) was only found in four of the C4 species sampled, while eight of the C4 species and all the C3 species have an alanine residue; indicating that this substitution is not a requirement for C4 function.
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