Protein Disulfide Isomerase as a Regulator of Chloroplast Translational Activation

  • Jungmook Kim
    Department of Cell Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
  • Stephen P. Mayfield
    Department of Cell Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

抄録

<jats:p> Light-regulated translation of chloroplast messenger RNAs (mRNAs) requires <jats:italic>trans-</jats:italic> acting factors that interact with the 5′ untranslated region (UTR) of these mRNAs. Chloroplast polyadenylate-binding protein (cPABP) specifically binds to the 5′-UTR of the <jats:italic>psbA</jats:italic> mRNA and is essential for translation of this mRNA. A protein disulfide isomerase that is localized to the chloroplast and copurifies with cPABP was shown to modulate the binding of cPABP to the 5′-UTR of the <jats:italic>psbA</jats:italic> mRNA by reversibly changing the redox status of cPABP through redox potential or adenosine 5′-diphosphate–dependent phosphorylation. This mechanism allows for a simple reversible switch regulating gene expression in the chloroplast. </jats:p>

収録刊行物

  • Science

    Science 278 (5345), 1954-1957, 1997-12-12

    American Association for the Advancement of Science (AAAS)

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