Protein Disulfide Isomerase as a Regulator of Chloroplast Translational Activation

作者：Jungmook Kim, Stephen Patrick Mayfield · 发表于：Science · 年份：1997 · DOI：10.1126/science.278.5345.1954 · 被引用次数：238 · 研究领域：Photosynthetic Processes and Mechanisms、Endoplasmic Reticulum Stress and Disease、Redox biology and oxidative stress

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.