Surveying Rubisco Diversity and Temperature Response to Improve Crop Photosynthetic Efficiency

Plant Physiol. 2016 Oct;172(2):707-717. doi: 10.1104/pp.16.00750. Epub 2016 Jun 24.

Abstract

The threat to global food security of stagnating yields and population growth makes increasing crop productivity a critical goal over the coming decades. One key target for improving crop productivity and yields is increasing the efficiency of photosynthesis. Central to photosynthesis is Rubisco, which is a critical but often rate-limiting component. Here, we present full Rubisco catalytic properties measured at three temperatures for 75 plants species representing both crops and undomesticated plants from diverse climates. Some newly characterized Rubiscos were naturally "better" compared to crop enzymes and have the potential to improve crop photosynthetic efficiency. The temperature response of the various catalytic parameters was largely consistent across the diverse range of species, though absolute values showed significant variation in Rubisco catalysis, even between closely related species. An analysis of residue differences among the species characterized identified a number of candidate amino acid substitutions that will aid in advancing engineering of improved Rubisco in crop systems. This study provides new insights on the range of Rubisco catalysis and temperature response present in nature, and provides new information to include in models from leaf to canopy and ecosystem scale.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocatalysis
  • Crops, Agricultural / classification
  • Crops, Agricultural / enzymology
  • Crops, Agricultural / genetics*
  • Genetic Variation*
  • Kinetics
  • Photosynthesis / genetics*
  • Phylogeny
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism
  • Ribulose-Bisphosphate Carboxylase / genetics*
  • Ribulose-Bisphosphate Carboxylase / metabolism
  • Sequence Analysis, DNA
  • Species Specificity
  • Temperature

Substances

  • Plant Proteins
  • RbcL protein, plastid
  • Ribulose-Bisphosphate Carboxylase