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Ghosh S, Gepstein S, Glick BR, et al. Thermal regulation of phosphoenolpyruvate carboxylase and ribulose-1,5-bisphosphate carboxylase in c(3) and c(4) plants native to hot and temperate climates. Plant Physiol. 1989;90(4):1298-304doi: 10.1104/pp.90.4.1298.
Ghosh, S., Gepstein, S., Glick, B. R., Heikkila, J. J., & Dumbroff, E. B. (1989). Thermal regulation of phosphoenolpyruvate carboxylase and ribulose-1,5-bisphosphate carboxylase in c(3) and c(4) plants native to hot and temperate climates. Plant physiology, 90(4), 1298-304. https://doi.org/10.1104/pp.90.4.1298
Ghosh, S, et al. "Thermal regulation of phosphoenolpyruvate carboxylase and ribulose-1,5-bisphosphate carboxylase in c(3) and c(4) plants native to hot and temperate climates." Plant physiology vol. 90,4 (1989): 1298-304. doi: https://doi.org/10.1104/pp.90.4.1298
Ghosh S, Gepstein S, Glick BR, Heikkila JJ, Dumbroff EB. Thermal regulation of phosphoenolpyruvate carboxylase and ribulose-1,5-bisphosphate carboxylase in c(3) and c(4) plants native to hot and temperate climates. Plant Physiol. 1989 Aug;90(4):1298-304. doi: 10.1104/pp.90.4.1298. PMID: 16666926; PMCID: PMC1061886.
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Plant Physiol. 1989 Aug;90(4):1298-304. doi: 10.1104/pp.90.4.1298.

Thermal regulation of phosphoenolpyruvate carboxylase and ribulose-1,5-bisphosphate carboxylase in c(3) and c(4) plants native to hot and temperate climates.

Plant physiology

S Ghosh, S Gepstein, B R Glick, J J Heikkila, E B Dumbroff

Affiliations

  1. Department of Biology, University of Waterloo, Waterloo, Ontario, N2L 3G1, Canada.

PMID: 16666926 PMCID: PMC1061886 DOI: 10.1104/pp.90.4.1298

Abstract

Exposure of leaf sections from 2-week-old seedlings of sorghum (Sorghum bicolor L.) (C(4) plant), corn (Zea mays L.) (C(4)), peanut (Arachis hypogaea L.) (C(3) plant), and soybean (Glycine max L.) (C(3)) to 40 or 45 degrees C for up to 4 hours resulted in significant increases in the levels of 102 kilodalton (C(4)), 52 kilodalton (C(3) and C(4)), and 15 kilodalton (C(3) and C(4)) polypeptides. These proteins comigrated, respectively, with authentic phosphoenolpyruvate carboxylase (PEPC) and the large (RLSU) and small (RSSU) subunits of ribulose-1,5-bisphosphate carboxylase (Rubisco) during both one- and two-dimensional SDS-PAGE and reacted with antisera raised against these enzymes. After 4 hours at 50 degrees C, levels of the polypeptides either remained relatively stable (PEPC, RLSU) or increased (RSSU) in sorghum and peanut (plants native to hot climates). In corn and soybean (plants native to temperate climates), levels of the proteins either fell sharply (corn) or showed strong evidence of incomplete processing and/or aggregation (soybean). In addition to changes in levels of the proteins, the activities of PEPC and Rubisco in extracts of leaves exposed to 50 degrees C fell by 84% and 11% of their respective control values in sorghum and by 54% each in peanut. In corn and soybean, the activities of both enzymes were depressed at 40 degrees C, with measured values at 50 degrees C not exceeding 5% of those from the nonstressed controls.

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