Protein Disulfide Isomerase as a Regulator of Chloroplast Translational Activation
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- Jungmook Kim
- Department of Cell Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
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- 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
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- Science
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Science 278 (5345), 1954-1957, 1997-12-12
American Association for the Advancement of Science (AAAS)
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詳細情報 詳細情報について
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- CRID
- 1361418520444134912
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- NII論文ID
- 80010062631
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- ISSN
- 10959203
- 00368075
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