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The High Light Response and Redox Control of Thylakoid FtsH Protease in Chlamydomonas reinhardtii
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2016 (Engelska)Ingår i: Mol PlantArtikel i tidskrift (Refereegranskat) Published
Abstract [en]

In Chlamydomonas reinhardtii, the major protease involved in the maintenance of the photosynthetic machinery in thylakoid membranes - the FtsH protease - forms mostly large hetero-oligomers ( approximately 1 MDa) comprising FtsH1 and FtsH2 subunits, whatever the light intensity for growth. Upon high light exposure, the FtsH subunits display a shorter half-life, which is counterbalanced by an increase in FTSH1/2 mRNA levels, resulting in a modest upregulation of FtsH1/2 proteins. Furthermore, we show that high light increases the protease activity through a hitherto unnoticed redox-controlled reduction of intermolecular disulfide bridges. We isolated a Chlamydomonas FTSH1 promoter deficient mutant, ftsh1-3, due to the insertion of a TOC1 transposon. Accordingly, the high light-induced upregulation of FTSH1 gene expression is largely lost. In this mutant, the abundance of the FtsH1 and 2 proteins are loosely coupled (respectively decreased by 70 and 30%) with no formation of large and stable homo-oligomers. Using strains exhibiting different accumulation levels of the FtsH1 subunit after complementation of the ftsh1-3 mutant, we demonstrate that high light tolerance is tightly correlated with the abundance of the FtsH protease. Thus, the response of Chlamydomonas to light stress involves higher levels of FtsH1/2 subunits associated into large complexes with increased proteolytic activity.

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2016.
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Biologiska vetenskaper
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URN: urn:nbn:se:umu:diva-144802ISBN: 1752-9867 (Electronic) 1674-2052 (Linking) OAI: oai:DiVA.org:umu-144802DiVA, id: diva2:1183512
Anmärkning

Wang, Fei Qi, Yafei Malnoe, Alizee Choquet, Yves Wollman, Francis-Andre de Vitry, Catherine ENG England 2016/10/06 06:00 Mol Plant. 2016 Oct 1. pii: S1674-2052(16)30221-0. doi: 10.1016/j.molp.2016.09.012.

Tillgänglig från: 2018-02-17 Skapad: 2018-02-17 Senast uppdaterad: 2018-06-09

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http://www.ncbi.nlm.nih.gov/pubmed/27702692

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Malnoë, A.

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