Characterization of a cDNA Clone for the PsaE Gene from Barley and Plasma Desorption Mass Spectrometry of the Corresponding Photosystem I Polypeptide PSI-E

  • Henrik Vibe Scheller
  • Jens Sigurd Okkels
  • Peter Roepstorff
  • Lars Bæk Jepsen
  • Birger Lindberg Møller


Photosystem I (PS I) preparations from barley contain polypeptides with apparent molecular masses of 82 (PSI-A and PSI-B), 18 (PSI-D), 16 (PSI-E), 14, 9.5 (PSI-H), 9 (PSI-C), 4, and 1.5 kDa (PSI-I) as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (1, 2). The nomenclature used for the subunits is described in more detail by Møller et al. (3). In this paper we report the characterization of a cDNA clone for the PsaE gene encoding the 16-kDa polypeptide PSI-E. The molecular mass of the mature polypeptide is 10,821 Da when deduced from the nucleotide sequence. To test whether the discrepancy between the molecular mass determinations could be due to post-translational modification of the polypeptide, the isolated polypeptide was analyzed by plasma desorption mass spectrometry. It has previously been established that the N- and C-terminal amino acid residues of the PSI-E polypeptide are not modified (4)


PsaE Gene Mature Polypeptide Plasma Desorption Mass Spectrometry Plasma Desorption Mass Spectrum 
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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Henrik Vibe Scheller
    • 1
  • Jens Sigurd Okkels
    • 1
  • Peter Roepstorff
    • 2
  • Lars Bæk Jepsen
    • 1
  • Birger Lindberg Møller
    • 1
  1. 1.Department of Plant PhysiologyRoyal Veterinary and Agricultural UniversityFrederiksberg CDenmark
  2. 2.Department of Molecular BiologyOdense UniversityOdenseDenmark

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