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Tausta, S Lori; Coyle, Heather Miller; Rothermel, Beverly A.; Stiefel, Virginia; Nelson, Timothy

doi:10.1023/a:1019998905615

Cited by 50 publications

(24 citation statements)

References 57 publications

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“…Different forms of some C 4 -related enzymes have different expression patterns, in terms of diurnal regulation and the tissues, cells, and subcellular compartments in which the enzyme is expressed (Maurino et al 1997; Finnegan et al 1999; Tausta et al 2002; Alvarez et al 2013). A function in C 4 photosynthesis requires light-induced high expression levels in specific cell types of the leaf (Sheen 1999).…”

Section: Discussionmentioning

confidence: 99%

“…In addition to expression patterns, the enzymes encoded by different members of the same gene family also differ in their catalytic properties (Ting and Osmond 1973; Tausta et al 2002; Svensson et al 2003; Alvarez et al 2013). In several of the C 4 -related genes, the evolution of C 4 -specific forms involved adaptive mutations of the coding sequence, which suggests catalytic modifications during the C 3 to C 4 transition (PEPC [Christin et al 2007; Wang et al 2009]; PCK [Christin, Petitpierre et al 2009]; NADP-ME [Christin, Samaritani et al 2009, Wang et al 2009]; CA, PPDK, PPDK-RP [Wang et al 2009]).…”

Section: Discussionmentioning

confidence: 99%

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Parallel Recruitment of Multiple Genes into C4 Photosynthesis

Christin¹,

Boxall²,

Gregory³

et al. 2013

Genome Biology and Evolution

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During the diversification of living organisms, novel adaptive traits usually evolve through the co-option of preexisting genes. However, most enzymes are encoded by gene families, whose members vary in their expression and catalytic properties. Each may therefore differ in its suitability for recruitment into a novel function. In this work, we test for the presence of such a gene recruitment bias using the example of C4 photosynthesis, a complex trait that evolved recurrently in flowering plants as a response to atmospheric CO2 depletion. We combined the analysis of complete nuclear genomes and high-throughput transcriptome data for three grass species that evolved the C4 trait independently. For five of the seven enzymes analyzed, the same gene lineage was recruited across the independent C4 origins, despite the existence of multiple copies. The analysis of a closely related C3 grass confirmed that C4 expression patterns were not present in the C3 ancestors but were acquired during the evolutionary transition to C4 photosynthesis. The significant bias in gene recruitment indicates that some genes are more suitable for a novel function, probably because the mutations they accumulated brought them closer to the characteristics required for the new function.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Parallel Recruitment of Multiple Genes into C4 Photosynthesis

Christin¹,

Boxall²,

Gregory³

et al. 2013

Genome Biology and Evolution

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“…For the constituent enzymes investigated so far, the new function requires alterations in the expression pattern and/or its catalytic properties (Finnegan et al , 1999; Tausta et al , 2002; Svensson et al , 2003; Gowik and Westhoff, 2011; Ludwig, 2011). For instance, the PEPC enzyme is ubiquitous in plants, where multiple isoforms are responsible for various non-photosynthetic functions (Lepiniec et al , 1994; Aubry et al , 2011; Gowik and Westhoff, 2011).…”

Section: Introductionmentioning

confidence: 99%

Shared origins of a key enzyme during the evolution of C4 and CAM metabolism

Christin

Arakaki

Osborne

et al. 2014

Journal of Experimental Botany

107

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“…9). This enzyme is constitutively expressed in maize and plays housekeeping roles; in contrast to the C 4 isoenzyme (8,9). By cloning and expressing both the maize plastidic photosynthetic (C 4 ) and non-photosynthetic NADP-ME (also known as non-C 4 -NADP-ME) as functional proteins in Escherichia coli, we identified several structural and kinetic differences between these two proteins (8,10).…”

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confidence: 99%

Identification of Domains Involved in Tetramerization and Malate Inhibition of Maize C4-NADP-Malic Enzyme

Detarsio¹,

Álvarez²,

Saigo³

et al. 2007

Journal of Biological Chemistry

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C 4 photosynthetic NADP-malic enzyme (ME) has evolved from non-C 4 isoforms and gained unique kinetic and structural properties during this process. To identify the domains responsible for the structural and kinetic differences between maize C 4 and non-C 4 -NADP-ME several chimeras between these isoforms were constructed and analyzed. By using this approach, we found that the region flanked by amino acid residues 102 and 247 is critical for the tetrameric state of C 4 -NADP-ME. In this way, the oligomerization strategy of these NADP-ME isoforms differs markedly from the one that present non-plant NADP-ME with known crystal structures. On the other hand, the region from residue 248 to the C-terminal end of the C 4 isoform is involved in the inhibition by high malate concentrations at pH 7.0. The inhibition pattern of the C 4 -NADP-ME and some of the chimeras suggested an allosteric site responsible for such behavior. This pH-dependent inhibition could be important for regulation of the C 4 isoform in vivo, with the enzyme presenting maximum activity while photosynthesis is in progress.

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Untitled

Cited by 50 publications

References 57 publications

Parallel Recruitment of Multiple Genes into C4 Photosynthesis

Parallel Recruitment of Multiple Genes into C4 Photosynthesis

Shared origins of a key enzyme during the evolution of C4 and CAM metabolism

Identification of Domains Involved in Tetramerization and Malate Inhibition of Maize C4-NADP-Malic Enzyme

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