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Science 12 December 1997: Vol. 278. no. 5345, pp. 1954 - 1957 DOI: 10.1126/science.278.5345.1954
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Reports
Protein Disulfide Isomerase as a Regulator of Chloroplast Translational Activation
Jungmook Kim,
Stephen P. Mayfield
Light-regulated translation of chloroplast messenger RNAs (mRNAs)
requires trans-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 psbA 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 psbA 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.
Department of Cell Biology and The Skaggs Institute for Chemical
Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
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