umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Thylakoid FtsH protease contributes to photosystem II and cytochrome b6f remodeling in Chlamydomonas  reinhardtii under stress conditions
Show others and affiliations
2014 (English)In: Plant Cell, Vol. 26, no 1, p. 373-90Article in journal (Refereed) Published
Abstract [en]

FtsH is the major thylakoid membrane protease found in organisms performing oxygenic photosynthesis. Here, we show that FtsH from Chlamydomonas reinhardtii forms heterooligomers comprising two subunits, FtsH1 and FtsH2. We characterized this protease using FtsH mutants that we identified through a genetic suppressor approach that restored phototrophic growth of mutants originally defective for cytochrome b6f accumulation. We thus extended the spectrum of FtsH substrates in the thylakoid membranes beyond photosystem II, showing the susceptibility of cytochrome b6f complexes (and proteins involved in the ci heme binding pathway to cytochrome b6) to FtsH. We then show how FtsH is involved in the response of C. reinhardtii to macronutrient stress. Upon phosphorus starvation, photosynthesis inactivation results from an FtsH-sensitive photoinhibition process. In contrast, we identified an FtsH-dependent loss of photosystem II and cytochrome b6f complexes in darkness upon sulfur deprivation. The D1 fragmentation pattern observed in the latter condition was similar to that observed in photoinhibitory conditions, which points to a similar degradation pathway in these two widely different environmental conditions. Our experiments thus provide extensive evidence that FtsH plays a major role in the quality control of thylakoid membrane proteins and in the response of C. reinhardtii to light and macronutrient stress.

Place, publisher, year, edition, pages
2014. Vol. 26, no 1, p. 373-90
Keywords [en]
ATP-Dependent Proteases/genetics/metabolism/*physiology, Algal Proteins/genetics/metabolism/*physiology, Chlamydomonas reinhardtii/*enzymology/genetics/metabolism, Cloning, Molecular, Cytochrome b6f Complex/*metabolism, Photosystem II Protein Complex/*metabolism, Point Mutation, *Stress, Physiological, Thylakoids/*metabolism
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:umu:diva-144807ISBN: 1532-298X (Electronic) 1040-4651 (Linking) OAI: oai:DiVA.org:umu-144807DiVA, id: diva2:1183506
Note

Malnoe, Alizee Wang, Fei Girard-Bascou, Jacqueline Wollman, Francis-Andre de Vitry, Catherine eng Research Support, Non-U.S. Gov't 2014/01/23 06:00 Plant Cell. 2014 Jan;26(1):373-90. doi: 10.1105/tpc.113.120113. Epub 2014 Jan 21.

Available from: 2018-02-17 Created: 2018-02-17 Last updated: 2018-06-09

Open Access in DiVA

No full text in DiVA

Other links

http://www.ncbi.nlm.nih.gov/pubmed/24449688

Authority records BETA

Malnoë, A.

Search in DiVA

By author/editor
Malnoë, A.
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar

isbn
urn-nbn

Altmetric score

isbn
urn-nbn
Total: 14 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf