Protein disulfide isomerase as a regulator of chloroplast translational activation

Protein disulfide isomerase as a regulator of chloroplast translational activation
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DOI:
10.1126/science.278.5345.1954
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发表时间:
1997-12-12
期刊:
影响因子:
56.9
通讯作者:
Mayfield, SP
Mayfield, SP
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Kim, JM;Mayfield, SP

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叶绿体信使rna (mRNAs)的光调节翻译需要与这些mRNA的5‘非翻译区(UTR)相互作用的交易因子,叶绿体多腺苷结合蛋白(cPABP)特异性结合psbA mRNA的5’-UTR,对该mRNA的翻译至关重要。一种定位于叶绿体并与cabp共同作用的蛋白质二硫异构酶被证明可以通过氧化还原电位或腺苷5'-二磷酸依赖性磷酸化可逆地改变cabp的氧化还原状态,从而调节cabp与psbA mRNA的5'-UTR的结合。这种机制允许一个简单的可逆开关调节叶绿体中的基因表达。
Light-regulated translation of chloroplast messenger RNAs (mRNAs) requires transacting 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.