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Comparison of hypothetical 3D-structures of Arabidopsis thaliana FtsH Proteases with the aim to predict FtsH complex formation
Umeå University, Faculty of Science and Technology, Department of Chemistry.
(English)Manuscript (preprint) (Other academic)
Abstract [en]

In Arabidopsis thaliana 12 metallo proteases of the FtsH family are located in the organellar membranes of chloroplasts and mitochondria. While it is known for the Arabidopsis FtsH proteases FtsH1, 2, 5 and 8 to form a hetero–oligomeric, hexameric complex in the chloroplast thylakoid membrane and for FtsH3 and 10 in the inner membrane of mitochondria, no data are available for the remaining (low abundant) FtsH proteases . We compared the sequence identity of amino acids predicted to be relevant in complex formation of FtsH proteases in order to predict additional hetero-oligomeric FtsH complexes. Focus was set on FtsH11 and FtsH4, two subunits that might form a complex in mitochondria. 

National Category
Chemical Sciences
URN: urn:nbn:se:umu:diva-55163OAI: diva2:525905
Available from: 2012-05-09 Created: 2012-05-09 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.



  • 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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Aigner, Harald
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Department of Chemistry
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