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Title | A male germ-cell-specific ribosome controls male fertility. |
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Journal, issue, pages | Nature, Vol. 612, Issue 7941, Page 725-731, Year 2022 |
Publish date | Dec 14, 2022 |
Authors | 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 / Jiahao Sha / |
PubMed Abstract | Ribosomes are highly sophisticated translation machines that have been demonstrated to be heterogeneous in the regulation of protein synthesis. Male germ cell development involves complex ...Ribosomes are highly sophisticated translation machines that have been demonstrated to be heterogeneous in the regulation of protein synthesis. Male germ cell development involves complex translational regulation during sperm formation. 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, Ribosome, that is assembled with the male germ-cell-specific protein RPL39L, the paralogue of core ribosome (Ribosome) protein RPL39. Deletion of Ribosome 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 Ribosome features a ribosomal polypeptide exit tunnel of distinct size and charge states compared with Ribosome. Ribosome 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 Ribosome were not replaceable by Ribosome. 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. |
External links | Nature / PubMed:36517592 |
Methods | EM (single particle) |
Resolution | 2.82 - 3.03 Å |
Structure data | EMDB-30432, PDB-7cpu: EMDB-30433, PDB-7cpv: |
Chemicals | ChemComp-MG: ChemComp-ZN: ChemComp-HOH: |
Source |
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Keywords | RIBOSOME / 80S mouse ribosome / protein translation / RPL39 / RPL39L / kidney ribosome / testis ribosome / Cryo-EM |