title: Photosynthetic flexibility in Pedilanthus tithymaloides poit, a CAM plant.
abstract: The induction of CAM in Pedilanthus tithymaloides (Euphorbiaceae) under water-limited conditions was evaluated by following diurnal oscillations of CO2 fixation, titratable acidity and malic acid content in the leaf extracts. CAM induction was assessed by measuring the activities of phosphoenolpyruvate carboxylase (PEPC), NADH-malate dehydrogenase (MDH) and phosphoenolpyruvate caroxykinase (PEPCK) in the leaves as well. Drought resulted in large increases in the nocturnal acid accumulation and rates of CO2 uptake in the leaves of P. tithymaloides. The drought-induced CAM activity tended to be reversible after re-watering. Nevertheless, under well-watered conditions, plants of P. tithymaloides showed day time CO2 uptake patterns with less pronounced diurnal oscillations of organic acids. Our data indicate that although P. tithymaloides is a CAM plant, environmental variables like drought induce photosynthetic flexibility in this species. This type of plasticity in CAM and metabolic versatility in P. tithymaloides should be an adaptation for prolonged survival under natural adverse edaphic and microclimate situations.
authors.affiliation: School of Life Sciences, Pondicherry University, Pondicherry 605 014, India. arreddy@yahoo.com
authors.forename: Attipalli Ramachandra
authors.initials: AR
authors.lastname: Reddy
authors.forename: Durai
authors.initials: D
authors.lastname: Sundar
authors.forename: Arumugam
authors.initials: A
authors.lastname: Gnanam
mesh_terms: D002245:Carbon Dioxide / Q000378:metabolism; D002940:Circadian Rhythm; D019665:Euphorbiaceae / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000378:metabolism; D008293:Malates / Q000378:metabolism; D010730:Phosphoenolpyruvate Carboxylase / Q000378:metabolism; D010788:Photosynthesis; D018515:Plant Leaves / Q000378:metabolism
chemical_list: D008293:Malates; D002245:Carbon Dioxide; C030298:malic acid; D008291:Malate Dehydrogenase; D010730:Phosphoenolpyruvate Carboxylase