A male germ-cell-specific ribosome controls male fertility

Huiling Li, Yangao Huo, Xi He, Liping Yao, Hao Zhang, Yiqiang Cui, Huijuan Xiao, Wenxiu Xie, Dejiu Zhang, Yue Wang, Shu Zhang, Haixia Tu, Yiwei Cheng, Yueshuai Guo, Xintao Cao, Yunfei Zhu, Tao Jiang, Xuejiang Guo (), Yan Qin () and Jiahao Sha ()
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Huiling Li: Nanjing Medical University
Yangao Huo: Chinese Academy of Sciences
Xi He: Nanjing Medical University
Liping Yao: Nanjing Medical University
Hao Zhang: Nanjing Medical University
Yiqiang Cui: Nanjing Medical University
Huijuan Xiao: Nanjing Medical University
Wenxiu Xie: Nanjing Medical University
Dejiu Zhang: Chinese Academy of Sciences
Yue Wang: Nanjing Medical University
Shu Zhang: Nanjing Medical University
Haixia Tu: Nanjing Medical University
Yiwei Cheng: Nanjing Medical University
Yueshuai Guo: Nanjing Medical University
Xintao Cao: Chinese Academy of Sciences
Yunfei Zhu: Nanjing Medical University
Tao Jiang: Chinese Academy of Sciences
Xuejiang Guo: Nanjing Medical University
Yan Qin: Chinese Academy of Sciences
Jiahao Sha: Nanjing Medical University

Nature, 2022, vol. 612, issue 7941, 725-731

Abstract: Abstract Ribosomes are highly sophisticated translation machines that have been demonstrated to be heterogeneous in the regulation of protein synthesis1,2. Male germ cell development involves complex translational regulation during sperm formation3. However, it remains unclear whether translation during sperm formation is performed by a specific ribosome. Here we report a ribosome with a specialized nascent polypeptide exit tunnel, RibosomeST, that is assembled with the male germ-cell-specific protein RPL39L, the paralogue of core ribosome (RibosomeCore) protein RPL39. Deletion of RibosomeST in mice causes defective sperm formation, resulting in substantially reduced fertility. Our comparison of single-particle cryo-electron microscopy structures of ribosomes from mouse kidneys and testes indicates that RibosomeST features a ribosomal polypeptide exit tunnel of distinct size and charge states compared with RibosomeCore. RibosomeST predominantly cotranslationally regulates the folding of a subset of male germ-cell-specific proteins that are essential for the formation of sperm. Moreover, we found that specialized functions of RibosomeST were not replaceable by RibosomeCore. Taken together, identification of this sperm-specific ribosome should greatly expand our understanding of ribosome function and tissue-specific regulation of protein expression pattern in mammals.

Date: 2022
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DOI: 10.1038/s41586-022-05508-0

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