A single serine to alanine substitution decreases bicarbonate affinity of phosphoenolpyruvate carboxylase in C4Flaveria trinervia

DiMario, Robert J.; Cousins, Asaph B.

doi:10.1093/jxb/ery403

Title: A single serine to alanine substitution decreases bicarbonate affinity of phosphoenolpyruvate carboxylase in C₄Flaveria trinervia

Journal Article · 04 December 2018 · Journal of Experimental Botany

DOI: https://doi.org/10.1093/jxb/ery403 · OSTI ID:1610566

DiMario, Robert J. ^[1]; Cousins, Asaph B. ^[2]

Washington State Univ., Pullman, WA (United States); DOE/OSTI
Washington State Univ., Pullman, WA (United States)

Phosphoenolpyruvate (PEP) carboxylase (PEPc) catalyzes the first committed step of C₄ photosynthesis generating oxaloacetate from bicarbonate (HCO₃^–) and PEP. It is hypothesized that PEPc affinity for HCO₃^– has undergone selective pressure for a lower K_HCO3 (K_m for HCO₃^–) to increase the carbon flux entering the C₄ cycle, particularly during conditions that limit CO₂ availability. However, the decrease in K_HCO3has been hypothesized to cause an unavoidable increase in K_PEP (K_m for PEP). Therefore, the amino acid residue S774 in the C₄ enzyme, which has been shown to increase K_PEP, should lead to a decrease in K_HCO3. Several studies reported the effect S774 has on K_PEP; however, the influence of this amino acid substitution on K_HCO3 has not been tested. To test these hypotheses, membrane-inlet mass spectrometry (MIMS) was used to measure the K_HCO3 of the photosynthetic PEPc from the C₄Flaveria trinervia and the non-photosynthetic PEPc from the C₃F. pringlei. The cDNAs for these enzymes were overexpressed and purified from the PEPc-less PCR1 Escherichia coli strain. Our work in comparison with previous reports suggests that K_HCO3 and K_PEP are linked by specific amino acids, such as S774; however, these kinetic parameters respond differently to the tested allosteric regulators, malate and glucose-6-phosphate.

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Research Organization:: Washington State University, Pullman, WA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division; National Science Foundation (NSF)

Grant/Contract Number:: SC0001685

OSTI ID:: 1610566

Journal Information:: Journal of Experimental Botany, Journal Name: Journal of Experimental Botany Journal Issue: 3 Vol. 70; ISSN 0022-0957

Publisher:: Oxford University PressCopyright Statement

Country of Publication:: United States

Language:: English

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Maize C4-form phosphoenolpyruvate carboxylase engineered to be functional in C3 plants: mutations for diminished sensitivity to feedback inhibitors and for increased substrate affinity Endo, T.; Mihara, Y.; Furumoto, T. Journal of Experimental Botany, Vol. 59, Issue 7 https://doi.org/10.1093/jxb/ern018	journal	June 2007
Positive selection of Kranz and non-Kranz C4 phosphoenolpyruvate carboxylase amino acids in Suaedoideae (Chenopodiaceae) Rosnow, Josh J.; Edwards, Gerald E.; Roalson, Eric H. Journal of Experimental Botany, Vol. 65, Issue 13 https://doi.org/10.1093/jxb/eru053	journal	March 2014
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In Vitro Phosphorylation of Maize Leaf Phosphoenolpyruvate Carboxylase Budde, Raymond J. A.; Chollet, Raymond Plant Physiology, Vol. 82, Issue 4 https://doi.org/10.1104/pp.82.4.1107	journal	December 1986
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Nitrogen acquisition, PEP carboxylase, and cellular pH homeostasis: new views on old paradigms Britto, Dev T.; Kronzucker, Herbert J. Plant, Cell and Environment, Vol. 28, Issue 11 https://doi.org/10.1111/j.1365-3040.2005.01372.x	journal	November 2005
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Simultaneous determination of Rubisco carboxylase and oxygenase kinetic parameters in Triticum aestivum and Zea mays using membrane inlet mass spectrometry Cousins, A. B.; Ghannoum, O.; Von Caemmerer, S. Plant, Cell & Environment, Vol. 33, Issue 3 https://doi.org/10.1111/j.1365-3040.2009.02095.x	journal	March 2010
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Two independent C ₄ origins in Aristidoideae (Poaceae) revealed by the recruitment of distinct phosphoenolpyruvate carboxylase genes Christin, Pascal-Antoine; Besnard, Guillaume American Journal of Botany, Vol. 96, Issue 12 https://doi.org/10.3732/ajb.0900111	journal	December 2009

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Title: A single serine to alanine substitution decreases bicarbonate affinity of phosphoenolpyruvate carboxylase in C4Flaveria trinervia

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Title: A single serine to alanine substitution decreases bicarbonate affinity of phosphoenolpyruvate carboxylase in C₄Flaveria trinervia