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Title | Structural basis for Gemin5 decamer-mediated mRNA binding. |
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Journal, issue, pages | Nat Commun, Vol. 13, Issue 1, Page 5166, Year 2022 |
Publish date | Sep 2, 2022 |
Authors | 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 / |
PubMed 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 ...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. |
External links | Nat Commun / PubMed:36056043 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.6 - 3.31 Å |
Structure data | EMDB-33152, PDB-7xdt: EMDB-33187, PDB-7xgr: |
Source |
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Keywords | RNA BINDING PROTEIN / RNA binding / TPR repeats / decamer / RNA translation |