umu.sePublikationer
Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Thylakoid FtsH protease contributes to photosystem II and cytochrome b6f remodeling in Chlamydomonas  reinhardtii under stress conditions
Visa övriga samt affilieringar
2014 (Engelska)Ingår i: Plant Cell, Vol. 26, nr 1, s. 373-90Artikel i tidskrift (Refereegranskat) 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.

Ort, förlag, år, upplaga, sidor
2014. Vol. 26, nr 1, s. 373-90
Nyckelord [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
Nationell ämneskategori
Biologiska vetenskaper
Identifikatorer
URN: urn:nbn:se:umu:diva-144807ISBN: 1532-298X (Electronic) 1040-4651 (Linking) OAI: oai:DiVA.org:umu-144807DiVA, id: diva2:1183506
Anmärkning

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.

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

Open Access i DiVA

Fulltext saknas i DiVA

Övriga länkar

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

Personposter BETA

Malnoë, A.

Sök vidare i DiVA

Av författaren/redaktören
Malnoë, A.
Biologiska vetenskaper

Sök vidare utanför DiVA

GoogleGoogle Scholar

isbn
urn-nbn

Altmetricpoäng

isbn
urn-nbn
Totalt: 50 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf