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AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).ORCID iD: 0000-0002-7906-6891
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2005 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 1091-6490, Vol. 102, no 39, 13699-704 p.Article in journal (Refereed) Published
Abstract [en]

Degradation of the most abundant membrane protein on earth, the light-harvesting complex of Photosystem II (LHC II), is highly regulated under various environmental conditions, e.g., light stress, to prevent photochemical damage to the reaction center. We identified the LHC II degrading protease in Arabidopsis thaliana as a Zn2+-dependent metalloprotease, activated by the removal of unknown extrinsic factors, similar to the proteolytic activity directed against Lhcb3 in barley. By using a reversed genetic approach, the chloroplast-targeted protease FtsH6 was identified as being responsible for the degradation. T-DNA KO A. thaliana mutants, lacking ftsH6, were unable to degrade either Lhcb3 during dark-induced senescence or Lhcb1 and Lhcb3 during highlight acclimation. The A. thaliana ftsH6 gene has a clear orthologue in the genome of Populus trichocarpa. It is likely that FtsH6 is a general LHC II protease and that FtsH6-dependent LHC II proteolysis is a feature of all higher plants.

Place, publisher, year, edition, pages
2005. Vol. 102, no 39, 13699-704 p.
Keyword [en]
membrane protein, photosynthesis, protease
URN: urn:nbn:se:umu:diva-13068DOI: doi:10.1073/pnas.0503472102OAI: diva2:152739
Available from: 2008-03-31 Created: 2008-03-31 Last updated: 2015-04-29Bibliographically approved
In thesis
1. The Role of Proteases in Plant Development
Open this publication in new window or tab >>The Role of Proteases in Plant Development
2007 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Proteases play key roles in plants, maintaining strict protein quality control and degrading specific sets of proteins in response to diverse environmental and developmental stimuli. Similarities and differences between the proteases expressed in different species may give valuable insights into their physiological roles and evolution.

Systematic comparative analysis of the available sequenced genomes of two model organisms led to the identification of an increasing number of protease genes, giving insights about protein sequences that are conserved in the different species, and thus are likely to have common functions in them and the acquisition of new genes, elucidate issues concerning non-functionalization, neofunctionalization and subfunctionalization.

The involvement of proteases in senescence and PCD was investigated. While PCD in woody tissues shows the importance of vacuole proteases in the process, the senescence in leaves demonstrate to be a slower and more ordered mechanism starting in the chloroplast where the proteases there localized become important.

The light-harvesting complex of Photosystem II is very susceptible to protease attack during leaf senescence. We were able to show that a metallo-protease belonging to the FtsH family is involved on the process in vitro. Arabidopsis knockout mutants confirmed the function of FtsH6 in vivo.

Place, publisher, year, edition, pages
Umeå: Kemi, 2007. 45 p.
Comparative genomics, protease, PCD, leaf senescence, FtsH, Arabidopsis, Populus
National Category
Biochemistry and Molecular Biology
urn:nbn:se:umu:diva-1386 (URN)978-91-7264-422-9 (ISBN)
Public defence
2007-10-26, KB3B1, KBC-huset, Linnaeus V. 6, Umeå, 13:00 (English)
Available from: 2007-10-05 Created: 2007-10-05 Last updated: 2009-09-08Bibliographically approved

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Jansson, StefanFunk, Christiane
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Department of ChemistryUmeå Plant Science Centre (UPSC)

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