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Degradation of the main Photosystem II light-harvesting complex
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
2005 (English)In: Photochemical and Photobiological Sciences, ISSN 1474-905X, Vol. 4, 1065-1071 p.Article in journal (Refereed) Published
Abstract [en]

Many factors trigger the degradation of proteins, including changes in environmental conditions, genetic mutations, and limitations in the availability of cofactors. Despite the importance for viability, still very little is known about protein degradation and its regulation. The degradation of the most abundant membrane protein on Earth, the light-harvesting complex of Photosystem II (LHC II), is highly regulated under different environmental conditions, e.g. light stress, to prevent photochemical damage of the reaction center. However, despite major effort to identify the protease/proteases involved in the degradation of the apoproteins of LHC II the molecular details of this important process remain obscure. LHC II belongs to the family of chlorophyll a/b binding proteins (CAB proteins) and is located in the thylakoid membrane of the plant chloroplast. The results of biochemical experiments to isolate and characterize the protease degrading LHC II are summarized here and compared to our own recent finding indicating that a metalloprotease of the FtsH family is involved in this process.

Place, publisher, year, edition, pages
2005. Vol. 4, 1065-1071 p.
URN: urn:nbn:se:umu:diva-14500DOI: doi:10.1039/b506625eOAI: diva2:154171
Available from: 2007-06-05 Created: 2007-06-05 Last updated: 2009-09-08Bibliographically 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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