Evolution of Phosphoenolpyruvate carboxylase encoding transcripts in Chickpea (Cicer arietinum L.)
Abstract
Background: Phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) is an important enzyme encoded by a gene family of at least 2-8 plant type and 1-2 bacterial type genes depending upon genome size or species complexity. This enzyme functions as catalyst for the β-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate in cytoplasm. It is involved in carbon fixation and various other plant metabolic pathways.
Methods: In this study we characterized the evolutionary perspective of PPC transcripts and their abundance pattern in different plant tissues of chickpea (Cicer arietinum L.).
Results: The current study revealed that PEPC enzyme in chickpea is encoded by a gene family of at least 6 transcripts. All active site residues of C3 PEPCs were found in transcripts. Phylogenetic analysis of the amino acid sequences showed two major groups PTPC and BTPC from different ancestral lineages. Divergence of PTPC in two groups and further convergence within species was found in most of the plants while multiple evolutionary divergences was likely to be specific in legumes including chickpea.
Conclusion: CaPPC genes are regulated under various abiotic stress. Furthermore, the expression pattern of the identified genes can be helpful to explore plant metabolism of chickpea under abiotic stresses, which can be the next step to explore more into this gene family in chickpea.
Keywords: Phosphoenolpyruvate carboxylase transcripts; Chickpea; Phylogeny
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Shah SRU, Agback P, Lundquist PO. Root morphology and cluster root formation by seabuckthorn (Hippophaë rhamnoides L.) in response to nitrogen, phosphorus and iron deficiency. Plant and soil, (2015); 397: (1-2) 75-91.
Latzko E, Kelly G. The many-faceted function of phosphoenolpyruvate carboxylase in C3 plants. Physiologie Végétale, (1983); 21: 805-15.
Izui K, Matsumura H, Furumoto T, Kai Y. Phosphoenolpyruvate carboxylase : a new era of structural biology Annual. Reviews. Plant Biology, (2004); 55: 69-84.
Plaxton, WC, Carswell, MC. Metabolic aspects of the phosphate starvation response in plants Plant responses to environmental stresses: from phytohormones to genome reorganization Marcel Dekker, New York, (1999); 349-372.
Shah SRU. Root system of seabuckthorn (Hippophaë rhamnoides L.). Diss. sammanfattning/summary) Uppsala: Sveriges lantbruksuniv., Acta Universitatis agriculturae Sueciae, (2015); 49: 1652-6880.
Theodorou ME, Plaxton WC. Metabolic adaptations of plant respiration to nutritional phosphate deprivation Plant physiology, (1993); 101: 339-344.
O’Leary B, et al. Tissue-specific expression and post-translational modifications of plant- and bacterial-type phosphoenolpyruvate carboxylase isozymes of the castor oil plant, Ricinus communis L. Journal of Experimental Botany, (2011); 62: 5485-95.
O’Leary B, Joonho P, William CP. The remarkable diversity of plant PEPC (phosphoenolpyruvate carboxylase): recent insights into the physiological functions and post-translational controls of non-photosynthetic PEPCs. Biochemical Journal, (2011); 436(1): 15-34.
Sánchez R, Cejudo FJ. Identification and expression analysis of a gene encoding a bacterial-type phosphoenolpyruvate carboxylase from Arabidopsis and Rice. Plant physiology, (2003); 132: 949-957.
Mamedov TG, Moellering ER, Chollet R. Identification and expression analysis of two inorganic C‐and N‐responsive genes encoding novel and distinct molecular forms of eukaryotic phosphoenolpyruvate carboxylase in the green microalga Chlamydomonas reinhardtii. The Plant Journal, (2005); 42: 832-843.
Muramatsu M, Suzuki R, Yamazaki T, Miyao M. Comparison of plant-type phosphoenolpyruvate carboxylases from rice: Identification of two plant-specific regulatory regions of the allosteric enzyme. Plant and Cell Physiology, (2014); 56: 468-80.
Masumoto C, et al. Phosphoenolpyruvate carboxylase intrinsically located in the chloroplast of rice plays a crucial role in ammonium assimilation Proceedings of the National Academy of Sciences, (2010); 107: 5226-5231.
Peñaloza E, Muñoz G, Salvo-Garrido H, Silva H, Corcuera LJ. Phosphate deficiency regulates phosphoenolpyruvate carboxylase expression in proteoid root clusters of white lupin Journal of Experimental Botany, (2005); 56: 145-153.
Gennidakis S, Rao S, Greenham K, Uhrig RG, O'Leary B, et al. Bacterial‐and plant‐type phosphoenolpyruvate carboxylase polypeptides interact in the hetero‐oligomeric Class‐2 PEPC complex of developing castor oil seeds. The Plant Journal, (2007); 52: 839-849.
Johnson JF, Vance CP, Allan DL. Phosphorus deficiency in Lupinus albus – Altered lateral root development and enhanced expression of phosphoenolpyruvate carboxylase. Plant physiology, (1996); 112: 31-41.
Peñaloza E, Corcuera LJ, Martinez J. Spatial and temporal variation in citrate and malate exudation and tissue concentration as affected by P stress in roots of white lupin Plant and Soil, (2002); 241: 209-221.
Fischinger SA, Hristozkova M, Mainassara ZA, Schulze J. Elevated CO2 concentration around alfalfa nodules increases N2 fixation Journal of experimental botany, (2010); 61: 121-130.
Wang N, Zhong X, Cong Y, et al. Genome-wide analysis of phosphoenolpyruvate carboxylase gene family and their Response to abiotic stresses in soybean. Scientific Reports, (2016); 6: 38448.
Qi X, Xu W, Zhang J, Guo R, Zhao M, et al. Physiological characteristics and metabolomics of transgenic wheat containing the maize C4 phosphoenolpyruvate carboxylase (PEPC) gene under high temperature stress. Protoplasma, (2017); 254: 1017–1030.
Qin N, Xu W, Hu L, Li Y, Wang H, et al. Drought tolerance and proteomics studies of transgenic wheat containing the maize C4 phosphoenolpyruvate carboxylase (PEPC) gene. Protoplasma, (2016); 253: 1503–1512.
Tamura K, Peterson D, Peterson N, Stecher G, Nei M, et al. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Molecular biology and evolution, (2011); 28: 2731-2739.
O’Leary B, Rao S, Plaxton W. Phosphorylation of bacterial-type phosphoenolpyruvate carboxylase at Ser425 provides a further tier of enzyme control in developing castor oil seeds. Biochemical Journal, (2011); 433(1): 65-74.
Sánchez R, Flores A, Cejudo FJ. Arabidopsis phosphoenolpyruvate carboxylase genes encode immunologically unrelated polypeptides and are differentially expressed in response to drought and salt stress. Planta, (2006); 223, 901-909.
Bläsing OE, Westhof P, Svensson P. Evolution of C4 phosphoenolpyruvate carboxylase in Flaveria, a conserved serine residue in the carboxyl-terminal part of the enzyme is a major determinant for C4-specific characteristics Journal of Biological Chemistry, (2000); 275: 27917-27923.
Paulus JK, Schlieper D, Groth G. Greater efficiency of photosynthetic carbon fixation due to single amino-acid substitution. Nature Communication. (2013); 4: 1518.
Igawa T, Fujiwara M, Tanaka I, Fukao Y, Yanagawa Y. Characterization of bacterial-type phosphoenolpyruvate carboxylase expressed in male gametophyte of higher plants. BMC Plant Biology, (2010); 10: 200.
Connell MB, Lee MJY, Li J, Plaxton WC, Jia Z. Structural and biochemical characterization of citrate binding to AtPPC3, a plant-type phosphoenolpyruvate carboxylase from Arabidopsis thaliana. Journal of Structural Biology, (2018); 204(3): 507-512.
Sangwan RS, Singh N, Plaxton WC. Phosphoenolpyruvate carboxylase activity and concentration in the endosperm of developing and germinating castor oil seeds Plant physiology, (1992); 99: 445-449.
Schmutz J, et al. Genome sequence of the paleopolyploid soybean. Nature, (2010); 463: 178-183.
Varshney RK, Song C, Saxena RK, et al. Draft genome sequence of chickpea (Cicer arietinum) provides a resource for trait improvement. Nature Biotechnology, (2013); 31, 240–246.
DOI: http://dx.doi.org/10.62940/als.v6i4.744
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