Umeå University's logo

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
Thioredoxin Interactions of the Chloroplast Lumen of Arabidopsis thaliana Indicate a Redox Regulation of the Xanthophyll Cycle
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).ORCID iD: 0000-0003-0864-9798
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
2008 (English)In: Photosynthesis: Energy from the Sun / [ed] Allen, J.F., Gantt, E., Golbeck, J.H., Osmond, B, Dordrecht: Springer, 2008, p. 1099-1102Conference paper, Published paper (Other academic)
Abstract [en]

Redox signalling via thioredoxins plays central roles in the light-mediated regulation of metabolic pathways of the chloroplast. Recent observations indicate strongly that thiotransduction pathways not only take place in the chloroplast stroma but also regulate functions of the chloroplast lumen. Thioredoxin signalling is probably an intrinsic characteristic of the entire chloroplast. Central questions are: (a) if there are thioredoxins or related proteins that can reduce luminal proteins, what are their sources of regeneration and their target proteins? (b) Are there links to other luminal pathways and how is redoxregulated luminal signal transduction coupled to the function of photosynthesis and signalling in the chloroplast stroma? This study aims to identify luminal thioredoxin targets and their biochemical functions. The initial experimental set-up using the E. coli thioredoxin/thioredoxin reductase system and fluorescence electrophoresis was able to confirm the known prevalent luminal thioredoxin targets that include PsbO1, PsbO2, TL17 and FKBP13. In addition, a novel thioredoxin interaction was observed for the enzyme violaxanthin deeopoxidase implying a role of luminal thioredoxin signals for regulation of the xanthophyll cycle.

Place, publisher, year, edition, pages
Dordrecht: Springer, 2008. p. 1099-1102
Keywords [en]
thioredoxin, chloroplast, thylakoid lumen, Arabidopsis thaliana, violaxanthin de-eopxidase, xanthophyll cycle
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-10013DOI: 10.1007/978-1-4020-6709-9_240ISBN: 978-1-4020-6707-5 (print)ISBN: 978-1-4020-6709-9 (electronic)OAI: oai:DiVA.org:umu-10013DiVA, id: diva2:149684
Conference
PS07, 14th International Congress on Photosynthesis, Glasgow, 2007
Available from: 2008-06-10 Created: 2008-06-10 Last updated: 2023-01-12Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full text

Authority records

Hall, MichaelSchröder, WolfgangKieselbach, Thomas

Search in DiVA

By author/editor
Hall, MichaelSchröder, WolfgangKieselbach, Thomas
By organisation
Department of ChemistryUmeå Plant Science Centre (UPSC)
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
isbn
urn-nbn

Altmetric score

doi
isbn
urn-nbn
Total: 296 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