Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco 
activases

Mueller-Cajar, Oliver; Stotz, Mathias; Bracher, Andreas

doi:10.1007/s11120-013-9819-0

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases

MPS-Authors

/persons/resource/persons77798

Bracher, Andreas
Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Mueller-Cajar, O., Stotz, M., & Bracher, A. (2014). Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases. Photosynthesis Research, 119(1-2), 191-201. doi:10.1007/s11120-013-9819-0.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0018-7AE0-7

Abstract

The key photosynthetic, CO2-fixing enzyme Rubisco forms inactivated complexes with its substrate ribulose 1,5-bisphosphate (RuBP) and other sugar phosphate inhibitors. The independently evolved AAA? proteins Rubisco activase and CbbX harness energy from ATP hydrolysis to remodel Rubisco complexes, facilitating release of these inhibitors. Here, we discuss recent structural and mechanistic advances towards the understanding of protein-mediated Rubisco activation. Both activating proteins appear to form ring-shaped hexameric arrangements typical for AAA? ATPases in their functional form, but display very different regulatory and biochemical properties. Considering the thermolability of the plant enzyme, an improved understanding of the mechanism for Rubisco activation may help in developing heat-resistant plants adapted to the challenge of global warming.