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FtsH11 protease is required for Arabidopsis thaliana to adapt to gtowth in continuous light
Umeå University, Faculty of Science and Technology, Department of Chemistry. (Christiane Funk)
Umeå University, Faculty of Science and Technology, Department of Chemistry.
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(English)Manuscript (preprint) (Other academic)
Abstract [en]

Continuous light can increase greenhouse food production; however, some of the most important greenhouse horticulture crops are not able to adapt to long photoperiods. Here, we provide evidence that knock-out of the FtsH11 protease causes molecular differences that prevent Arabidopsis thaliana to adapt to prolonged photoperiods. Previously this protease had been shown to be critical for thermotolerance (Chen et al. 2006). We demonstrate that knock-out mutants deficient of FtsH11 develop chlorosis when shifted to continuous light. When grown under normal growth conditions and short days, ftsh11 displayed changes in protein amount of chloroplast proteins involved in the photosynthetic light reaction and the Calvin cycle as well as of the FtsH12 protease. The proteomic changes are accompanied by reduced non-photochemical quenching and faster state transition. A shift to continuous light further enhanced these effects and induced morphological changes of the chloroplast and chlorosis. No changes in the mitochondrial proteome were observed between wild type and ftsh11.

Keyword [en]
FtsH 11 protease, continuous light, Calvin cycle, NADP+, ROS, chlorosis.
National Category
Biological Sciences
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:umu:diva-54614OAI: oai:DiVA.org:umu-54614DiVA: diva2:525884
Available from: 2012-05-09 Created: 2012-05-02 Last updated: 2012-10-24Bibliographically approved
In thesis
1. Characterization of FtsH proteases in the annual plant Arabidopsis thaliana
Open this publication in new window or tab >>Characterization of FtsH proteases in the annual plant Arabidopsis thaliana
2012 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Background FtsH is an ATP-dependent membrane-bound metalloprotease. A. thaliana contains 12 FtsH proteases localized in membranes of chloroplasts and mitochondria where they form homo- or hetero-hexameric complexes. FtsH11 – the main subject of this thesis – is located in the chloroplast envelope.

 

Methods

  • Field studies with A. thaliana to determine Darwinian fitness. A growth under outdoor conditions often allows discovering of phenotypes that are unascertainable in the controlled environment of growth chambers.
  • Proteomic methods to discover fragments of substrate proteins (limited proteolysis) and changes in the proteome of FtsH protease deficient mutants.

 

Results ftsh11 has increased amount of: RuBisCO activase, several Calvin cycle enzymes, two enzymes involved in starch synthesis and some chaperons. Some of those enzymes have been identified as possible substrates of FtsH11. Under long photoperiods ftsh11 develops a chlorotic phenotype accompanied by decreasing NADP+/NADPH ratio and increase of ROS damaged proteins. 

Place, publisher, year, edition, pages
Umeå: Umeå universitet, 2012. 38 p.
National Category
Biological Sciences Chemical Sciences
Research subject
Biochemistry
Identifiers
urn:nbn:se:umu:diva-55161 (URN)978-91-7459-445-4 (ISBN)
Public defence
2012-06-01, KBC-huset, KB3A9, Umeå universitet, Umeå, 10:00 (English)
Opponent
Supervisors
Available from: 2012-05-11 Created: 2012-05-09 Last updated: 2012-05-10Bibliographically approved

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Aigner, HaraldWagner, RaikFunk, Christiane
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