Protein disulfide isomerase as a regulator of chloroplast translational activation
- Skaggs Institute for Chemical Biology, La Jolla, CA (United States)
Light-regulated translation of chloroplast messenger RNAs (mRNAs) requires transacting factors that interact with the 5{prime} untranslated region (UTR) of these mRNAs. Chloroplast polyadenylate-binding protein (cPABP) specifically binds to the 5{prime}-UTR of the psbA mRNA and is essential for translation of this mRNA. A protein disulfide isomeriase that is localized to the chloroplast and copurifies with cPABP was shown to modulate the binding of cPABP to the 5{prime}-UTR of the psbA mRNA by reversibly changing the redox status of cPaBP through redox potential or adenosine 5{prime}-diphosphate-dependent phosphorylation. This mechanism allows for a simple reversible switch regulating gene expression in the chloroplast. 23 refs., 5 figs.
- OSTI ID:
- 569480
- Journal Information:
- Science, Journal Name: Science Journal Issue: 5345 Vol. 278; ISSN SCIEAS; ISSN 0036-8075
- Country of Publication:
- United States
- Language:
- English
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