Functional involvement of Tudor and dPRMT5 in the piRNA processing pathway in Drosophila germlines

Functional involvement of Tudor and dPRMT5 in the piRNA processing pathway in Drosophila germlines
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DOI:
10.1038/emboj.2009.365
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发表时间:
2009-12-16
期刊:
影响因子:
11.4
通讯作者:
Siomi, Mikiko C.
Siomi, Mikiko C.
中科院分区:
生物学1区
文献类型:
--
作者:
Nishida, Kazumichi M.;Okada, Tomoko N.;Siomi, Mikiko C.

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在果蝇中,PIWI 蛋白、茄子蛋白 (Aub)、AGO3 和 Piwi 在种系中表达,并通过与 PIWI 相互作用 RNA (piRNA) 结合而发挥沉默转座子的功能。最近的研究表明,PIWI 蛋白含有对称二甲基精氨酸 (sDMA),而 dPRMT5/Capsuleen/DART5 是修饰酶。在这里,我们表明 Tudor (Tud)(一种含有 Tud 结构域的蛋白质)与 Aub 和 AGO3 结合,特别是通过它们的 sDMA 修饰,并且这三种蛋白质形成异聚复合物。在这些复合物中检测到 piRNA 前体样分子。 Aub 和 AGO3 的表达水平及其 sDMA 修饰程度并未因 tud 突变而改变。然而,与 Aub 和 AGO3 相关的转座子衍生的 piRNA 数量因 tud 突变而改变,而 Aub 和 AGO3 上的小 RNA 总量却增加了。 dprmt5 的缺失不会改变 Aub 的稳定性,但会损害其与 Tud 的关联,并降低 piRNA 与 Aub 的关联。因此,在生殖细胞中,piRNA 由 dPRMT5 进行质量控制,dPRMT5 修饰 PIWI 蛋白,与 Tud 密切相关。 EMBO 杂志 (2009) 28, 3820-3831。 doi:10.1038/emboj.2009.365; 2009 年 12 月 3 日在线发布
In Drosophila, the PIWI proteins, Aubergine (Aub), AGO3, and Piwi are expressed in germlines and function in silencing transposons by associating with PIWI-interacting RNAs (piRNAs). Recent studies show that PIWI proteins contain symmetric dimethyl-arginines (sDMAs) and that dPRMT5/Capsuleen/DART5 is the modifying enzyme. Here, we show that Tudor (Tud), one of Tud domain-containing proteins, associates with Aub and AGO3, specifically through their sDMA modifications and that these three proteins form heteromeric complexes. piRNA precursor-like molecules are detected in these complexes. The expression levels of Aub and AGO3, along with their degree of sDMA modification, were not changed by tud mutations. However, the population of transposon-derived piRNAs associated with Aub and AGO3 was altered by tud mutations, whereas the total amounts of small RNAs on Aub and AGO3 was increased. Loss of dprmt5 did not change the stability of Aub, but impaired its association with Tud and lowered piRNA association with Aub. Thus, in germline cells, piRNAs are quality-controlled by dPRMT5 that modifies PIWI proteins, in tight association with Tud. The EMBO Journal (2009) 28, 3820-3831. doi: 10.1038/emboj.2009.365; Published online 3 December 2009