Structure of the Gene (tmpA) for the “32,000-Mr” Thylakoid Membrane Polypeptide of Spinacia Oleracea and Nicotiana Debneyi

  • G. Zurawski
  • H.-J. Bohnert
  • P. R. Whitfeld
  • W. Bottomley
Part of the NATO Advanced Science Institutes Series book series (NSSA, volume 63)


One of the most rapidly labeled products of chloroplast protein synthesis is a polypeptide of Mr 32,000–36,0001,2,3,4. It is synthesized as a precursor of Mr 33,500–34,5003,4 and does not accumulate in the organelle but is rapidly turned over4. Recently the polypeptide has been shown to be involved in the binding of the herbicides atrazine and DCMU and to be part of Photosystem II with a role in electron flow5. The gene (tmpA) for this polypeptide has been mapped on the chloroplast genome of a number of plant species. In spinach, as in most other plants so far studied, tmpA is located in the large single copy region of the chloroplast genome very close to the end of one of the inverted repeat regions6.


Chloroplast Genome Spinach Chloroplast Spinacia OLERACEA Herbicide Atrazine Large Single Copy Region 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    G.E. Blair and R.J. Ellis Protein synthesis in chloroplasts 1. Light-driven synthesis of the large subunit of Fraction 1 protein by isolated pea chloroplasts, Biochim. Biophys. Acta 319: 223 (1973).PubMedGoogle Scholar
  2. 2.
    W. Bottomley, D. Spencer and P.R. Whitfeld Protein synthesis in isolated chloroplasts: Comparison of light-driven and ATP-driven synthesis, Arch. Biochem. Biophys. 164: 186 (1974).CrossRefGoogle Scholar
  3. 3.
    A.E. Grebanier, D.M. Coen, A. Rich and L. Bogorad Membrane proteins synthesized but not processed by isolated maize chloroplasts, J. Cell Biol. 78: 734 (1978).PubMedCrossRefGoogle Scholar
  4. 4.
    M. Edelman and A. Reisfeld, Characterization, translation and control of the 32,000 dalton chloroplast membrane protein in Spivodela, in “Chloroplast Development” G. Akoyunoglou and J.H. Argyroudi-Akoyunoglou, eds. Elsevier North-Holland, Amsterdam, New York (1978).Google Scholar
  5. 5.
    K.E. Steinback, L. McIntosh, L. Bogorad and C.J. Arntzen Identification of the triazine receptor protein as a chloroplast gene product, Proc. Natl. Acad. Soi. USA 78: 7463 (1981).CrossRefGoogle Scholar
  6. 6.
    A.J. Driesel, J. Speirs and H.-J. Bohnert Spinach chloroplast mRNA for a 32,000 dalton polypeptide. Size and localization on the physical map of the chloroplast DNA, Biochem. Biophys. Acta 610: 297 (1980).PubMedGoogle Scholar
  7. 7.
    M.R. Hartley, A. Wheeler and R.J. Ellis Protein synthesis in chloroplasts V Translation of messenger RNA for the large subunit of Fraction 1 protein in a heterologous cell-free system, J. Mol. Biol. 91: 67 (1975).PubMedCrossRefGoogle Scholar
  8. 8.
    G. von Heijne On the hydrophobic nature of signal sequences, Eur. J. Bioohem. 116: 419 (1981).CrossRefGoogle Scholar
  9. 9.
    M. Rosenberg and D. Court Regulatory sequences involved in the promotion and termination of RNA transcription, Ann. Rev. Genet. 13: 319 (1979).PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • G. Zurawski
    • 1
    • 2
  • H.-J. Bohnert
    • 1
    • 3
  • P. R. Whitfeld
    • 1
  • W. Bottomley
    • 1
  1. 1.CSIRO, Division of Plant IndustryCanberra CityAustralia
  2. 2.DNAX Research InstitutePalo AltoUSA
  3. 3.M.P.I. ZüchtungsforschungCologneGermany

Personalised recommendations