The pentatricopeptide repeat-SMR protein ATP4 promotes translation of the chloroplast atpB/E mRNA.

The pentatricopeptide repeat-SMR protein ATP4 promotes translation of the chloroplast atpB/E mRNA.
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五肽重复 SMR 蛋白 ATP4 促进叶绿体 atpB/E mRNA 的翻译

DOI:
10.1111/j.1365-313x.2012.05081.x
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发表时间:
2012
期刊:
The Plant journal : for cell and molecular biology
影响因子:
--
通讯作者:
Schmitz-Linneweber C
Schmitz-Linneweber C
中科院分区:
--
文献类型:
--
作者:
Zoschke R;Kroeger T;Belcher S;Schöttler MA;Barkan A;Schmitz-Linneweber C

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核基因产物对叶绿体翻译的调控是调控叶绿体基因表达的重要手段,但其机制尚不清楚。我们在玉米中描述了一个五肽重复(PPR)蛋白,ATP4,这是翻译叶绿体pbopen阅读框所必需的。我们证明了ATP4在体内与theatpB/EmRNA异常长5 ‘ UTR的5 ’末端附近的序列结合,它促进了核糖体与该mRNA的结合,并且它是叶绿体ATP合成酶的积累和活性所必需的。ATP4是多功能的,因为它也增强了ATP4的翻译,并且是积累特定的procsedatpfandpsajtranscripts所必需的。ATP4属于PPR蛋白的一个亚类,包括一个小的MutS相关(SMR)结构域。SMR结构域以前主要与DNA相关的功能相关,但我们的研究结果表明,至少一些PPR - SMR蛋白可以作用于RNA。ATP4与拟南芥蛋白SVR7是同源的,但ATP4和SVR7突变体的表型表明,这些同源物的功能并没有严格保守。
The regulation of chloroplast translation by nuclear gene products makes a major contribution to the control of chloroplast gene expression, but the underlying mechanisms are poorly understood. We describe a pentatricopeptide repeat (PPR) protein in maize, ATP4, that is necessary for translation of the chloroplastatpBopen reading frame. We demonstrate that ATP4 associatesin vivowith sequences near the 5′ end of the unusually long 5′ UTR of theatpB/EmRNA, that it facilitates ribosome association with this mRNA, and that it is required for accumulation and activity of the chloroplast ATP synthase. ATP4 is multifunctional, in that it also enhancesatpAtranslation and is required for accumulation of specific processedatpFandpsaJtranscripts. ATP4 belongs to a sub‐class of PPR proteins that include a small MutS‐related (SMR) domain. SMR domains had previously been associated primarily with DNA‐related functions, but our findings imply that at least some PPR‐SMR proteins can act on RNA. ATP4 is orthologous to the Arabidopsis protein SVR7, but the phenotypes ofatp4andsvr7mutants suggest that the functions of these orthologs have not been strictly conserved.
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