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 role of lhca complexes in the supramolecular organization of higher plant photosystem I
Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).ORCID iD: 0000-0002-7906-6891
Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Show others and affiliations
2009 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 284, no 12, 7803-7810 p.Article in journal (Refereed) Published
Abstract [en]

In this work, Photosystem I supercomplexes have been purified from Lhca-deficient lines of Arabidopsis thaliana using a mild detergent treatment that does not induce loss of outer antennas. The complexes have been studied by integrating biochemical analysis with electron microscopy. This allows the direct correlation of changes in protein content with changes in supramolecular structure of Photosystem I to get information about the position of the individual Lhca subunits, the association of the antenna to the core, and the influence of the individual subunits on the stability of the system. Photosystem I complexes with only two or three antenna complexes were purified, showing that the binding of Lhca1/4 and Lhca2/3 dimers to the core is not interdependent, although weak binding of Lhca2/3 to the core is stabilized by the presence of Lhca4. Moreover, Lhca2 and Lhca4 can be associated with the core in the absence of their "dimeric partners." The structure of Photosystem I is very rigid, and the absence of one antenna complex leaves a "hole" in the structure that cannot be filled by other Lhcas, clearly indicating that the docking sites for the individual subunits are highly specific. There is, however, an exception to the rule: Lhca5 can substitute for Lhca4, yielding highly stable PSI supercomplexes with a supramolecular organization identical to the WT.

Place, publisher, year, edition, pages
American Society for Biochemistry and Molecular Biology, 2009. Vol. 284, no 12, 7803-7810 p.
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-22111DOI: 10.1074/jbc.M808395200PubMedID: 19139095OAI: oai:DiVA.org:umu-22111DiVA: diva2:212700
Available from: 2009-04-23 Created: 2009-04-23 Last updated: 2017-12-13Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Jansson, Stefan
By organisation
Department of Plant PhysiologyUmeå Plant Science Centre (UPSC)
In the same journal
Journal of Biological Chemistry
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 55 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