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Fitness analyses of Arabidopsis thaliana mutants depleted of FtsH metalloproteases and characterization of three FtsH6 deletion mutants exposed to high light stress, senescence and chilling
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Plant Physiology.
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2011 (English)In: New Phytologist, ISSN 0028-646X, E-ISSN 1469-8137, Vol. 191, no 2, 449-458 p.Article in journal (Refereed) Published
Abstract [en]

Darwinian fitness analyses were performed, comparing single ftsh mutants with wild-type Arabidopsis thaliana plants grown under controlled laboratory conditions and in the field, by measuring plant size, survival rate, and silique and seed production.

 Additionally, three genotypes of ΔFtsH6 were analysed, under controlled growth conditions, with respect to both their ability to degrade the light-harvesting complex of photosystem II during senescence and light acclimation.

In the field, substantial increases in variegation and reductions in growth were observed in the ΔFtsH2, ΔFtsH5 and ΔFtsH10 mutants; FtsH2 seemed particularly important for plant survival. Despite being grown in relatively cold weather, the ΔFtsH11 mutant displayed strong phenotypic deviations from wild type. Both ΔFtsH10 and ΔFtsH3 mutants exhibited less severe phenotypic changes, but were different from wild-type plants when placed in the field as young plants. When older ΔFtsH3 or ΔFtsH10 mutants were placed outdoors, no phenotypic differences from wild type were observed. Three genotypes of ΔFtsH6 displayed no phenotypic deviations from wild-type plants.

Under controlled growth conditions, during senescence and light acclimation, no differences in the amount of chlorophyll or Photosystem II light-harvesting complex b3 (Lhcb3) were detected in ΔFtsH6 mutants compared with the wild type. Therefore, FtsH6 seems to be unimportant for LHCII degradation in vivo.

Place, publisher, year, edition, pages
Wiley , 2011. Vol. 191, no 2, 449-458 p.
Keyword [en]
AAA-type protease, Arabidopsis thaliana, fitness, freeland, FtsH, phenotype
National Category
Chemical Sciences
URN: urn:nbn:se:umu:diva-42190DOI: 10.1111/j.1469-8137.2011.03684.xPubMedID: 21438879OAI: diva2:408867
Available from: 2011-04-06 Created: 2011-04-06 Last updated: 2015-04-29Bibliographically 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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Wagner, RaikAigner, HaraldPružinská, AdrianaJohansson Jänkänpää, HannaJansson, StefanFunk, Christiane
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Department of ChemistryDepartment of Plant PhysiologyUmeå Plant Science Centre (UPSC)
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New Phytologist
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