Multifunctional RNA Binding Protein OsTudor-SN in Storage Protein mRNA Transport and Localization

Multifunctional RNA Binding Protein OsTudor-SN in Storage Protein mRNA Transport and Localization
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DOI:
10.1104/pp.17.01388
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发表时间:
2017-12-01
期刊:
影响因子:
7.4
通讯作者:
Okita, Thomas W.
Okita, Thomas W.
中科院分区:
生物学1区
文献类型:
--
作者:
Chou, Hong-Li;Tian, Li;Okita, Thomas W.

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多功能RNA结合蛋白Tudor-SN在转录和转录后过程中起着多种作用,这是由于其模块化结构域结构,由四个串联的葡萄球菌核酸酶(SN)样结构域(4SN),随后是羧基末端Tudor结构域,随后是第五部分SN序列(Tsn)组成。在植物中,它赋予胁迫耐受性,是胁迫颗粒和P-体的组分,并可能参与稳定和定位RNA到发育中的水稻(Oryza sativa)胚乳的皮质内质网的特定亚结构域。在这里,我们表明,除了完整的水稻OsTudor-SN蛋白,4SN和Tsn模块作为独立的多肽存在,它们可以共同组装形成一个复杂的人口的同源二聚体和异源双链体物种。4SN和Tsn模块在RNA结合中表现出不同的作用,并作为应激相关蛋白和RNA结合蛋白的蛋白质支架。尽管它们具有不同的个体特性,但4SN和Tsn模块中的突变将储存蛋白mRNA错误定位于皮质内质网。这些结果表明,OsTudor-SN的两个模块肽区域赋予不同的细胞特性,但在mRNA定位中合作,这是一个连接其在细胞核和细胞质中的多种功能的过程。
The multifunctional RNA-binding protein Tudor-SN plays multiple roles in transcriptional and posttranscriptional processes due to its modular domain structure, consisting of four tandem Staphylococcus nuclease (SN)-like domains (4SN), followed by a carboxyl-terminal Tudor domain, followed by a fifth partial SN sequence (Tsn). In plants, it confers stress tolerance, is a component of stress granules and P-bodies, and may participate in stabilizing and localizing RNAs to specific subdomains of the cortical-endoplasmic reticulum in developing rice (Oryza sativa) endosperm. Here, we show that, in addition to the intact rice OsTudor-SN protein, the 4SN and Tsn modules exist as independent polypeptides, which collectively may coassemble to form a complex population of homodimer and heteroduplex species. The 4SN and Tsn modules exhibit different roles in RNA binding and as a protein scaffold for stress-associated proteins and RNA-binding proteins. Despite their distinct individual properties, mutations in both the 4SN and Tsn modules mislocalize storage protein mRNAs to the cortical endoplasmic reticulum. These results indicate that the two modular peptide regions of OsTudor-SN confer different cellular properties but cooperate in mRNA localization, a process linking its multiple functions in the nucleus and cytoplasm.