HSP90α plays an important role in piRNA biogenesis and retrotransposon repression in mouse.
HSP90α plays an important role in piRNA biogenesis and retrotransposon repression in mouse.
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DOI：
10.1093/nar/gku881
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发表时间：
2014-10-29
影响因子：
14.9
通讯作者：
Udono H
中科院分区：
文献类型：
--
作者：
Ichiyanagi T;Ichiyanagi K;Ogawa A;Kuramochi-Miyagawa S;Nakano T;Chuma S;Sasaki H;Udono H
HSP 90广泛存在于生命的各个领域，是一种主要的伴侣蛋白，调节许多客户蛋白。HSP 90 α是脊椎动物中复制的两种旁系同源物之一，在小鼠雄性生殖细胞中对转座子活性起作用的胎儿PIWI相互作用RNA（皮尔纳）的生物合成中起重要作用。Hsp 90 α的敲除突变导致初级和次级piRNA表达的大幅降低以及PIWI同源物MIWI 2的错误定位。而编码共伴侣蛋白的Fkbp 6中的突变减少了28-32个核苷酸长度的piRNA，Hsp 90 α突变减少了24-32个核苷酸的piRNA，表明存在HSP 90 α的FKBP 6依赖性和非依赖性作用。虽然在Hsp 90 α突变体睾丸中DNA甲基化和L1反转录转座子的mRNA水平基本上没有变化，但L1编码的蛋白质增加，表明存在转录后调控。这项研究揭示了HSP 90 α亚型在哺乳动物雄性生殖细胞发育过程中皮尔纳生物合成和逆转录转座子抑制中的专门功能。
HSP90, found in all kingdoms of life, is a major chaperone protein regulating many client proteins. We demonstrated that HSP90α, one of two paralogs duplicated in vertebrates, plays an important role in the biogenesis of fetal PIWI-interacting RNAs (piRNA), which act against the transposon activities, in mouse male germ cells. The knockout mutation of Hsp90α resulted in a large reduction in the expression of primary and secondary piRNAs and mislocalization of MIWI2, a PIWI homolog. Whereas the mutation in Fkbp6 encoding a co-chaperone reduced piRNAs of 28–32 nucleotides in length, the Hsp90α mutation reduced piRNAs of 24–32 nucleotides, suggesting the presence of both FKBP6-dependent and -independent actions of HSP90α. Although DNA methylation and mRNA levels of L1 retrotransposon were largely unchanged in the Hsp90α mutant testes, the L1-encoded protein was increased, suggesting the presence of post-transcriptional regulation. This study revealed the specialized function of the HSP90α isofom in the piRNA biogenesis and repression of retrotransposons during the development of male germ cells in mammals.
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影响因子：
1.7
作者：
Jurka, J;Kapitonov, VV;Walichiewicz, J
通讯作者：
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影响因子：
30.8
作者：
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影响因子：
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影响因子：
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作者：
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通讯作者：
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