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Chloroplastic prenylated proteins

I Parmryd1, C A Shipton, E Swiezewska

  • 1Department of Biochemistry, Stockholm University, Sweden. ingela@biokemi.su.se

FEBS Letters
|October 10, 1997
PubMed
Summary
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This study provides evidence for protein prenylation in spinach chloroplasts, identifying prenylated polypeptides and their membrane localization. Farnesyl protein transferase activity was detected in the thylakoid membrane.

Area of Science:

  • Plant molecular biology
  • Chloroplast biochemistry
  • Protein modification

Background:

  • Protein prenylation is a crucial post-translational modification.
  • Its presence and function in plant chloroplasts remain largely unexplored.

Purpose of the Study:

  • To investigate the existence and characteristics of protein prenylation within spinach chloroplasts.
  • To identify prenylated proteins and their subcellular localization.

Main Methods:

  • In vivo [3H]mevalonate labeling of spinach plants.
  • Biochemical analysis including SDS-PAGE and autoradiography.
  • Thermolysin treatment of intact chloroplasts to assess surface localization.

Main Results:

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  • Approximately 20 prenylated polypeptides were identified in chloroplasts.
  • 40% of these were localized to the cytoplasmic surface of the outer envelope membrane.
  • The remaining prenylated polypeptides were found in thylakoids and/or the inner envelope membrane, often within larger protein complexes.
  • Farnesyl protein transferase activity was associated with the thylakoid membrane.
  • Conclusions:

    • Protein prenylation occurs in spinach chloroplasts, involving multiple polypeptides.
    • Prenylated proteins are distributed across different chloroplast compartments, including envelope membranes and thylakoids.
    • The presence of farnesyl protein transferase activity suggests a functional prenylation pathway within the thylakoid membrane.