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The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein
Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
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2000 (English)In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 12, no 3, 419-431 p.Article in journal (Refereed) Published
Abstract [en]

The photosystem II reaction center D1 protein is known to turn over frequently. This protein is prone to irreversible damage caused by reactive oxygen species that are formed in the light, the damaged, nonfunctional D1 protein is degraded and replaced by a new copy. However, the proteases responsible for D1 protein degradation remain unknown. In this study, we investigate the possible role of the FtsH protease, an ATP-dependent zinc metalloprotease, during this process. The primary light-induced cleavage product of the D1 protein, a 23-kD fragment, was found to be degraded in isolated thylakoids in the dark during a process dependent on ATP hydrolysis and divalent metal ions, suggesting the involvement of FtsH. Purified FtsH degraded the 23-kD D1 fragment present in isolated photosystem II core complexes, as well as that in thylakoid membranes depleted of endogenous FtsH. In this study, we definitively identify the chloroplast protease acting on the D1 protein during its light-induced turnover. Unlike previously identified membrane-bound substrates for FtsH in bacteria and mitochondria, the 23-kD D1 fragment represents a novel class of FtsH substrate - functionally assembled proteins that have undergone irreversible photooxidative damage and cleavage.

Place, publisher, year, edition, pages
2000. Vol. 12, no 3, 419-431 p.
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Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-24865DOI: 10.1105/tpc.12.3.419Local ID: 9267OAI: oai:DiVA.org:liu-24865DiVA: diva2:245188
Available from: 2009-10-07 Created: 2009-10-07 Last updated: 2017-12-13

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Spetea, CorneliaHundal, TorillAndersson, Bertil

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