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Structural basis for arginine methylation-independent recognition of PIWIL1 by TDRD2.


ABSTRACT: The P-element-induced wimpy testis (PIWI)-interacting RNA (piRNA) pathway plays a central role in transposon silencing and genome protection in the animal germline. A family of Tudor domain proteins regulates the piRNA pathway through direct Tudor domain-PIWI interactions. Tudor domains are known to fulfill this function by binding to methylated PIWI proteins in an arginine methylation-dependent manner. Here, we report a mechanism of methylation-independent Tudor domain-PIWI interaction. Unlike most other Tudor domains, the extended Tudor domain of mammalian Tudor domain-containing protein 2 (TDRD2) preferentially recognizes an unmethylated arginine-rich sequence from PIWI-like protein 1 (PIWIL1). Structural studies reveal an unexpected Tudor domain-binding mode for the PIWIL1 sequence in which the interface of Tudor and staphylococcal nuclease domains is primarily responsible for PIWIL1 peptide recognition. Mutations disrupting the TDRD2-PIWIL1 interaction compromise piRNA maturation via 3'-end trimming in vitro. Our work presented here reveals the molecular divergence of the interactions between different Tudor domain proteins and PIWI proteins.

SUBMITTER: Zhang H 

PROVIDER: S-EPMC5703303 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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Structural basis for arginine methylation-independent recognition of PIWIL1 by TDRD2.

Zhang Heng H   Liu Ke K   Izumi Natsuko N   Huang Haiming H   Ding Deqiang D   Ni Zuyao Z   Sidhu Sachdev S SS   Chen Chen C   Tomari Yukihide Y   Min Jinrong J  

Proceedings of the National Academy of Sciences of the United States of America 20171108 47


The P-element-induced wimpy testis (PIWI)-interacting RNA (piRNA) pathway plays a central role in transposon silencing and genome protection in the animal germline. A family of Tudor domain proteins regulates the piRNA pathway through direct Tudor domain-PIWI interactions. Tudor domains are known to fulfill this function by binding to methylated PIWI proteins in an arginine methylation-dependent manner. Here, we report a mechanism of methylation-independent Tudor domain-PIWI interaction. Unlike  ...[more]

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