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Gemin5 in the Survival Motor Neuron (SMN) complex serves as the RNA-binding protein to deliver small nuclear RNAs (snRNAs) to the small nuclear ribonucleoprotein Sm complex via its N-terminal WD40 domain. Additionally, the C-terminal region plays an important role in regulating RNA translation by directly binding to viral RNAs and cellular mRNAs. Here, we present the three-dimensional structure of the Gemin5 C-terminal region, which adopts a homodecamer architecture comprised of a dimer of pentamers. By structural analysis, mutagenesis, and RNA-binding assays, we find that the intact pentamer/decamer is critical for the Gemin5 C-terminal region to bind cognate RNA ligands and to regulate mRNA translation. The Gemin5 high-order architecture is assembled via pentamerization, allowing binding to RNA ligands in a coordinated manner. We propose a model depicting the regulatory role of Gemin5 in selective RNA binding and translation. Therefore, our work provides insights into the SMN complex-independent function of Gemin5. © 2022. The Author(s).

Citation

Qiong Guo, Shidong Zhao, Rosario Francisco-Velilla, Jiahai Zhang, Azman Embarc-Buh, Salvador Abellan, Mengqi Lv, Peiping Tang, Qingguo Gong, Huaizong Shen, Linfeng Sun, Xuebiao Yao, Jinrong Min, Yunyu Shi, Encarnacion Martínez-Salas, Kaiming Zhang, Chao Xu. Structural basis for Gemin5 decamer-mediated mRNA binding. Nature communications. 2022 Sep 02;13(1):5166

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PMID: 36056043

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