Structural basis for RNA 3 '-end recognition by the PIWIL2 PAZ domain
Structural basis for RNA 3 '-end recognition by the PIWIL2 PAZ domain
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DOI：
10.1016/j.bbrc.2021.03.080
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发表时间：
2021
影响因子：
3.1
通讯作者：
Xu Chao
中科院分区：
文献类型：
--
作者：
Li Qianqian;Dong Aiping;Zhu Zhongliang;Zhang Jiahai;Li Yanjun;Xu Chao
Piwi家族蛋白是ArgAerte家族的重要成员，当携带piRNAs时，在精子发生和发育中发挥重要作用。在这里，我们解决了人PIWIL2PAZ结构域的晶体结构，发现它的PAZ结构域采用了典型的PAZ折叠。我们进一步建立了PIWIL2与2和3‘突起结合的同源模型。我们发现PIWIL2利用一个深疏水凹面来容纳RNA 3‘端的2个核苷酸。PIWIL2对2和3‘端突出物的识别在其他人PIWIL蛋白中也是保守的，这意味着PAZ结构域在与靶RNA结合方面具有进化上的保守作用。
PIWI family proteins are important members of Argonaute family that play an essential role in spermatogenesis and development when loaded with piRNAs. Here we solved the crystal structure of the human PIWIL2 PAZ domain and found its PAZ domain adopts a canonical PAZ fold. We furhter built a homology model of PIWIL2 bound to 2 nt 3′ overhangs. We found that PIWIL2 utilizes a deep hydrophobic concave to accommodate the 2 nt at 3′-end of RNAs. The recognition of 2 nt 3′ overhangs by PIWIL2 is conserved in other human PIWIL proteins, implicating the evolutionarily conserved role of PAZ domain in binding to target RNAs.