Mueller-Cajar, Oliver and Stotz, Mathias and Bracher, Andreas (2014) Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases. PHOTOSYNTHESIS RESEARCH, 119 (1-2). pp. 191-201. ISSN 0166-8595, 1573-5079
Full text not available from this repository. (Request a copy)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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | RIBULOSE-BISPHOSPHATE CARBOXYLASE; MODERATE HEAT-STRESS; ALGA CYANIDIOSCHYZON-MEROLAE; NUCLEOTIDE-BINDING POCKET; FORM I RUBISCO; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE; 1,5-BISPHOSPHATE CARBOXYLASE; RIBULOSEBISPHOSPHATE CARBOXYLASE; ENCODED CBBX; 2-CARBOXYARABINITOL 1-PHOSPHATE; Rubisco; Activase; AAA plus proteins; CbbX; CO2-assimilation |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I > Prof. Dr. Gunter Meister |
| Depositing User: | Petra Gürster |
| Date Deposited: | 21 Jul 2020 09:48 |
| Last Modified: | 21 Jul 2020 09:48 |
| URI: | https://pred.uni-regensburg.de/id/eprint/10778 |
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