Protein disulfide isomerase as a regulator of chloroplast translational activation.
basic_science · Level V
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Abstract
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.
Medical subject headings
- Chlamydomonas reinhardtii
- Chloroplasts
- Gene Expression Regulation
- Protein Biosynthesis
- Protein Disulfide-Isomerases
- RNA-Binding Proteins