FEBS Letters
Volume 582, Issue 2 , Pages 249-254, 23 January 2008

Single particle analysis of thylakoid proteins from Thermosynechococcus elongatus and Synechocystis 6803: Localization of the CupA subunit of NDH-1

Edited by Richard Cogdell

  • I. Mihaela Folea

      Affiliations

    • Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
    • ,
  • Pengpeng Zhang

      Affiliations

    • Department of Biology, University of Turku, FIN-20014 Turku, Finland
    • ,
  • Marc M. Nowaczyk

      Affiliations

    • Plant Biochemistry, Faculty of Biology, Ruhr-University Bochum, 44801 Bochum, Germany
    • ,
  • Teruo Ogawa

      Affiliations

    • Department of Biology, University of Turku, FIN-20014 Turku, Finland
    • ,
  • Eva-Mari Aro

      Affiliations

    • Department of Biology, University of Turku, FIN-20014 Turku, Finland
    • ,
  • Egbert J. Boekema

      Affiliations

    • Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
    • Corresponding Author InformationCorresponding author. Fax: +31 50 3634800.

Received 12 November 2007; received in revised form 5 December 2007; accepted 6 December 2007. published online 14 December 2007.

Abstract 

The larger protein complexes of the cyanobacterial photosynthetic membrane of Thermosynechoccus elongatus and Synechocystis 6803 were studied by single particle electron microscopy after detergent solubilization, without any purification steps. Besides the “standard” L-shaped NDH-1L complex, related to complex I, large numbers of a U-shaped NDH-1MS complex were found in both cyanobacteria. In membranes from Synechocystis ΔcupA and ΔcupA/cupB mutants the U-shaped complexes were absent, indicating that CupA is responsible for the U-shape by binding at the tip of the membrane-bound arm of NDH-1MS. Comparison of membranes grown under air levels of CO2 or 3% CO2 indicates that the number of NDH-1MS particles is 30-fold higher under low-CO2.

Abbreviations: HC, high-CO2 (3% or 5%), LC, low-CO2 (air level)

Keywords: Electron microscopy, Single particle analysis, Membrane protein, NDH-1, CupA, Thermosynechococcus elongatus, Synechocystis 6803

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PII: S0014-5793(07)01271-9

doi:10.1016/j.febslet.2007.12.012

FEBS Letters
Volume 582, Issue 2 , Pages 249-254, 23 January 2008

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