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Rubisco kinetic acclimation at the holoenzyme level.

Bryce Askey1, Maddie Ceminsky1, Elena Scott2

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Area of Science:

  • Plant biochemistry
  • Enzyme kinetics
  • Structural biology

Background:

  • Rubisco, the CO2-fixing enzyme, is crucial for photosynthesis.
  • Plants utilize multiple small subunits (SSus) for Rubisco holoenzymes.
  • SSu diversity may enable Rubisco's kinetic acclimation to environmental changes.

Purpose of the Study:

  • To investigate the structural and kinetic plasticity of Rubisco.
  • To determine if Rubisco holoenzymes are heterogeneous in small subunit composition.
  • To understand how SSu heterogeneity influences Rubisco's catalytic properties.

Main Methods:

  • Characterization of Rubisco in Arabidopsis thaliana.
  • Quantification of SSu heterogeneity in Rubisco holoenzymes.
  • Kinetic analysis of different SSu compositions.
  • Cryo-electron microscopy (cryo-EM) for structural insights.

Main Results:

  • SSu-heterogeneous Rubisco constitutes over half of the Rubisco pool in heterologous expression.
  • At least four unique SSu ratios were identified, indicating diverse holoenzyme arrangements.
  • SSu heterogeneity impacts substrate and inhibitor affinity, correlating with local flexibility.
  • A warm-temperature SSu variant showed increased active site stability and substrate affinity.

Conclusions:

  • Rubisco holoenzymes exhibit significant SSu heterogeneity in Arabidopsis thaliana.
  • This heterogeneity allows for fine-tuning of Rubisco's kinetic properties.
  • Structural flexibility and local stability of SSus are key mechanisms for kinetic acclimation.