Structural basis for Gemin5 decamer-mediated mRNA binding

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 () and Chao Xu ()
Additional contact information
Qiong Guo: University of Science and Technology of China
Shidong Zhao: University of Science and Technology of China
Rosario Francisco-Velilla: CSIC-UAM
Jiahai Zhang: University of Science and Technology of China
Azman Embarc-Buh: CSIC-UAM
Salvador Abellan: CSIC-UAM
Mengqi Lv: University of Science and Technology of China
Peiping Tang: University of Science and Technology of China
Qingguo Gong: University of Science and Technology of China
Huaizong Shen: Westlake University
Linfeng Sun: University of Science and Technology of China
Xuebiao Yao: University of Science and Technology of China
Jinrong Min: University of Toronto
Yunyu Shi: University of Science and Technology of China
Encarnacion Martínez-Salas: CSIC-UAM
Kaiming Zhang: University of Science and Technology of China
Chao Xu: University of Science and Technology of China

Nature Communications, 2022, vol. 13, issue 1, 1-10

Abstract: Abstract 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.

Date: 2022
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DOI: 10.1038/s41467-022-32883-z

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