Chaperones for the Folding, Assembly, and Activation of RuBisCO — ASN Events
  1. Schedule
  2. Session Fifteen - Protein Dynamics, Folding and Misfolding
  3. Chaperones for the Folding, Assembly, and Activation of RuBisCO

Chaperones for the Folding, Assembly, and Activation of RuBisCO (#39)

Manajit Hayer-Hartl 1
  1. Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany

Life on earth is dependent on the ability of photosynthetic organisms to sequester inorganic carbon dioxide of the atmosphere into organic carbon via the Calvin-Benson-Bassham (CBB) cycle. The key enzyme responsible for this process is ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), the most abundant protein in nature. It is also arguably the most important protein, since all biomass, and thus all food source, results either directly or indirectly from the action of RuBisCO. Despite its central role in biomass production, RuBisCO is an inefficient enzyme and also catalyses the wasteful reaction of photorespiration (oxygen as the substrate instead of carbon dioxide). Recent forecasts suggest that global food production will need to rise more than 30% by 2050 to meet the ever increasing demand of the growing human population. Hence, engineering a more efficient RuBisCO enzyme will be important to increase agricultural output and may also be useful in controlling the greenhouse gas induced climate change. However, efforts to evolve RuBisCO must take into account the complex cellular pathways and machineries for its folding, assembly and activation. I will discuss our recent structural and functional analysis of the molecular chaperones that mediate RuBisCO biogenesis and maintenance, specifically the assembly chaperone RbcX and the AAA+ chaperone RuBisCO activase.

  1. Saschenbrecker, S., Bracher, A., Vasudeva Rao, K., Vasudeva Rao, B., Hartl, F.U. and Hayer-Hartl, M. (2007). Structure and Function of RbcX, a specific assembly chaperone for hexadecameric Rubisco. Cell 129, 1189-1200.
  2. Liu, C., Young, A.L., Starling-Windhof, A., Bracher, A., Saschenbrecker, S., Rao, B.V., Rao, K.V., Berninghausen, O., Mielke, T., Hartl, F.U., Beckmann, R. and Hayer-Hartl, M. (2010). Coupled chaperone action in folding and assembly of hexadecameric Rubisco. Nature 463, 197-202.
  3. Bracher, A., Starling-Windhof, A., Hartl, F.U., and Hayer-Hartl, M. (2011). Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco. Nat. Struct. Mol. Biol. 18, 875-880.
  4. Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F.U., Bracher, A., and Hayer-Hartl, M. (2011). Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase. Nature 479, 194-199.
  5. Stotz, M., Mueller-Cajar, O., Ciniawsky, S., Wendler, P., Hartl, F.U., Bracher, A., and Hayer-Hartl, M. (2011). Structure of green-type Rubisco activase from tobacco. Nat. Struct. Mol. Biol. 18, 1366-1370.