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
The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome.
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
2006 (English)In: FEBS Letters, ISSN 0014-5793, Vol. 580, no 26, 6055-61 p.Article in journal (Refereed) Published
Abstract [en]

Peroxiredoxins have been discovered in many organisms ranging from eubacteria to mammals, and their known biological functions include both oxidant defense and signal transduction. The genome of Arabidopsis thaliana encodes for ten individual peroxiredoxins, of which four are located in the chloroplast. The best-characterized member of the chloroplast peroxiredoxins is 2-Cys Prx that is associated with the stroma side of the thylakoid membrane and is considered to participate in antioxidant defense and protection of photosynthesis. This study addressed the chloroplast peroxiredoxin Prx Q and showed that its subcellular location is the lumen of the thylakoid membrane. To get insight in the biological function of the Prx Q protein of Arabidopsis, the protein levels of the Prx Q protein in thylakoid membranes were studied under different light conditions and oxidative stress. A T-DNA knockout mutant of Prx Q did not show any visible phenotype and had normal photosynthetic performance with a slightly increased oxygen evolving activity.

Place, publisher, year, edition, pages
2006. Vol. 580, no 26, 6055-61 p.
Keyword [en]
Arabidopsis Proteins, Chloroplasts/*chemistry/metabolism, Light, Oxidative Stress, Oxygen/metabolism, Peroxidases/*analysis/genetics/physiology, Proteome, Thylakoids/chemistry
Identifiers
URN: urn:nbn:se:umu:diva-11793DOI: doi:10.1016/j.febslet.2006.10.001PubMedID: 17054949OAI: oai:DiVA.org:umu-11793DiVA: diva2:151464
Available from: 2008-04-08 Created: 2008-04-08 Last updated: 2009-09-15Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=17054949&dopt=Citation

Search in DiVA

By author/editor
Kieselbach, Thomas
By organisation
Chemistry

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 72 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