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  Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-7AE0-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-7AEB-2
Genre: Journal Article

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 Creators:
Mueller-Cajar, Oliver1, Author              
Stotz, Mathias1, Author              
Bracher, Andreas2, Author              
Affiliations:
1External Organizations, ou_persistent22              
2Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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Free keywords: Rubisco Activase AAA? proteins CbbX CO2-assimilation
 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.

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Language(s): eng - English
 Dates: 2013-03-312014-02
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s11120-013-9819-0
 Degree: -

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Title: Photosynthesis Research
  Alternative Title : Photosynthesis and the Environment
Source Genre: Journal
 Creator(s):
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Publ. Info: New York : Springer
Pages: - Volume / Issue: 119 (1-2) Sequence Number: - Start / End Page: 191 - 201 Identifier: ISSN: 0166-8595
ISSN: 1573-5079
CoNE: https://pure.mpg.de/cone/journals/resource/954925482637