Sensitivity of photosynthesis in a C4 plant, maize, to heat stress.
Our objective was to determine the sensitivity of components of the photosynthetic apparatus of maize (Zea mays), a C4 plant, to high temperature stress. Net photosynthesis (Pn) was inhibited at leaf temperatures above 38 degrees C, and the inhibition was much more severe when the temperature was increased rapidly rather than gradually. Transpiration rate increased progressively with leaf temperature, indicating that inhibition was not associated with stomatal closure. Nonphotochemical fluorescence quenching (qN) increased at leaf temperatures above 30 degrees C, indicating increased thylakoid energization even at temperatures that did not inhibit Pn. Compared with CO(2) assimilation, the maximum quantum yield of photosystem II (F(v)/F(m)) was relatively insensitive to leaf temperatures up to 45 degrees C. The activation state of phosphoenolpyruvate carboxylase decreased marginally at leaf temperatures above 40 degrees C, and the activity of pyruvate phosphate dikinase was insensitive to temperature up to 45 degrees C. The activation state of Rubisco decreased at temperatures exceeding 32.5 degrees C, with nearly complete inactivation at 45 degrees C. Levels of 3-phosphoglyceric acid and ribulose-1,5-bisphosphate decreased and increased, respectively, as leaf temperature increased, consistent with the decrease in Rubisco activation. When leaf temperature was increased gradually, Rubisco activation acclimated in a similar manner as Pn, and acclimation was associated with the expression of a new activase polypeptide. Rates of Pn calculated solely from the kinetics of Rubisco were remarkably similar to measured rates if the calculation included adjustment for temperature effects on Rubisco activation. We conclude that inactivation of Rubisco was the primary constraint on the rate of Pn of maize leaves as leaf temperature increased above 30 degrees C.
Crafts-Brandner
Steven J
SJ
Western Cotton Research Laboratory, United States Department of Agriculture-Agricultural Research Service, Phoenix, Arizona 85040-8803, USA. scraftsbrandner@wcrl.ars.edu
Salvucci
Michael E
ME
D000064:Acclimatization / Q000502:physiology*; D002245:Carbon Dioxide / Q000378:metabolism; D004789:Enzyme Activation / Q000502:physiology; D005988:Glyceric Acids / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000096:biosynthesis; D006358:Hot Temperature; D010730:Phosphoenolpyruvate Carboxylase / Q000378:metabolism; D010788:Photosynthesis / Q000502:physiology* / Q000528:radiation effects; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism / Q000528:radiation effects; D045332:Photosystem II Protein Complex; D018515:Plant Leaves / Q000502:physiology; D018526:Plant Transpiration / Q000502:physiology; D011772:Pyruvate, Orthophosphate Dikinase / Q000378:metabolism; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism; D012274:Ribulosephosphates / Q000378:metabolism; D020524:Thylakoids / Q000502:physiology; D003313:Zea mays / Q000502:physiology*
D005988:Glyceric Acids; D006360:Heat-Shock Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D012274:Ribulosephosphates; D002245:Carbon Dioxide; C001933:ribulose-1,5 diphosphate; C005156:3-phosphoglycerate; D011772:Pyruvate, Orthophosphate Dikinase; D010730:Phosphoenolpyruvate Carboxylase; D012273:Ribulose-Bisphosphate Carboxylase