Scafaro, Andrew and Gallé, Alexander and van Rie, Jeroen and Carmo-Silva, Ana Elizabete and Salvucci, Michael E. and Atwell, Brian J. (2016) Heat tolerance in a wild Oryza species is attributed to maintenance of Rubisco activation by a thermally stable Rubisco activase ortholog. New Phytologist, 211 (3). pp. 899-911. ISSN 0028-646X
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Abstract
• The response of photosynthesis and plant growth to short periods of supra-optimal heat was tested in rice (Oryza sativa) and two wild Oryza species from the Australian savanna, O. meridionalis and O. australiensis. The mechanism of heat tolerance in the wild species was explored, particularly focusing on the heat-labile protein Rubisco activase (RCA). • We compared leaf elongation rates, net photosynthesis and Rubisco activation state at moderate (28°C) and high temperature (45°C). Sequence analysis followed by enzyme kinetics of RCA was used to identify structural differences and thermal stability. • Oryza australiensis was the most heat-tolerant species. Rubisco activation state was positively correlated with leaf elongation rates across all three species at four times following exposure to 45°C. Oryza australiensis had multiple polymorphisms in the RCA primary protein sequence, and the protein was thermally stable up to 42°C relative to RCA from O. sativa which became inhibited at 36°C. • We attribute the heat tolerance of growth and photosynthesis in these wild species to thermal stability of RCA, enabling Rubisco to remain active. Because thermal stability of RCA in O. australiensis co-occurs with reduced enzyme specific activity, an increased RCA to Rubisco ratio is required in vivo to maintain high Rubisco activation.