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Searching for substrates of the metallo protease FtsH11 of Arabidopsis thaliana using N-terminal proteomics
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2012 (English)Manuscript (preprint) (Other academic)
Abstract [en]

FtsH11 is a membrane-bound metalloprotease localized in mitochondria and in the chloroplast envelope of Arabidopsis thaliana. An ftsh11 knock-out mutant has been shown to develop a chlorotic phenotype in prolonged photoperiods. The proteome of the ftsh11 chloroplast revealed increased abundance of several Calvin cycle enzymes, chaperones and some other proteins, however, none of those proteins could be verified to be an FtsH11 substrate (Harald Aigner, Raik Wagner, Lars L.E. Sjögren, Holger Eubel, A. Harvey Millar, Adrian K. Clarke, Christiane Funk, 2012, manuscript submitted). Here, we have used positional proteomics to identify peptides that report FtsH11 processing events. In this work we were able to identify seven chloroplast-localized proteins that are processed in wild type, but not in ftsh11.  

Place, publisher, year, edition, pages
National Category
Chemical Sciences
URN: urn:nbn:se:umu:diva-55162OAI: diva2:525902
Available from: 2012-05-09 Created: 2012-05-09 Last updated: 2012-05-10Bibliographically 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.



  • 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
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)
Available from: 2012-05-11 Created: 2012-05-09 Last updated: 2012-05-10Bibliographically approved

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