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The | ==Cryo-EM structure of 80S ribosome from mouse kidney== | ||
<StructureSection load='7cpu' size='340' side='right'caption='[[7cpu]], [[Resolution|resolution]] 2.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7cpu]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CPU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.82Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7cpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cpu OCA], [https://pdbe.org/7cpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cpu RCSB], [https://www.ebi.ac.uk/pdbsum/7cpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cpu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RS15A_MOUSE RS15A_MOUSE] Component of the small ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (By similarity). Required for proper erythropoiesis (By similarity).[UniProtKB:P62244]<ref>PMID:36517592</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ribosomes are highly sophisticated translation machines that have been demonstrated to be heterogeneous in the regulation of protein synthesis(1,2). Male germ cell development involves complex translational regulation during sperm formation(3). 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(ST), that is assembled with the male germ-cell-specific protein RPL39L, the paralogue of core ribosome (Ribosome(Core)) protein RPL39. Deletion of Ribosome(ST) 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(ST) features a ribosomal polypeptide exit tunnel of distinct size and charge states compared with Ribosome(Core). Ribosome(ST) 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(ST) were not replaceable by Ribosome(Core). 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. | |||
A male germ-cell-specific ribosome controls male fertility.,Li H, Huo Y, He X, Yao L, Zhang H, Cui Y, Xiao H, Xie W, Zhang D, Wang Y, Zhang S, Tu H, Cheng Y, Guo Y, Cao X, Zhu Y, Jiang T, Guo X, Qin Y, Sha J Nature. 2022 Dec;612(7941):725-731. doi: 10.1038/s41586-022-05508-0. Epub 2022 , Dec 14. PMID:36517592<ref>PMID:36517592</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7cpu" style="background-color:#fffaf0;"></div> | ||
[[Category: Guo | |||
[[Category: He | ==See Also== | ||
[[Category: | *[[Ribosome 3D structures|Ribosome 3D structures]] | ||
[[Category: | *[[3D sructureseceptor for activated protein kinase C 1|3D sructureseceptor for activated protein kinase C 1]] | ||
[[Category: Sha | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Guo XJ]] | |||
[[Category: He X]] | |||
[[Category: Huo YG]] | |||
[[Category: Jiang T]] | |||
[[Category: Qin Y]] | |||
[[Category: Sha JH]] |
Latest revision as of 22:30, 29 May 2024
Cryo-EM structure of 80S ribosome from mouse kidneyCryo-EM structure of 80S ribosome from mouse kidney
Structural highlights
FunctionRS15A_MOUSE Component of the small ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (By similarity). Required for proper erythropoiesis (By similarity).[UniProtKB:P62244][1] Publication Abstract from PubMedRibosomes are highly sophisticated translation machines that have been demonstrated to be heterogeneous in the regulation of protein synthesis(1,2). Male germ cell development involves complex translational regulation during sperm formation(3). 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(ST), that is assembled with the male germ-cell-specific protein RPL39L, the paralogue of core ribosome (Ribosome(Core)) protein RPL39. Deletion of Ribosome(ST) 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(ST) features a ribosomal polypeptide exit tunnel of distinct size and charge states compared with Ribosome(Core). Ribosome(ST) 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(ST) were not replaceable by Ribosome(Core). 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. A male germ-cell-specific ribosome controls male fertility.,Li H, Huo Y, He X, Yao L, Zhang H, Cui Y, Xiao H, Xie W, Zhang D, Wang Y, Zhang S, Tu H, Cheng Y, Guo Y, Cao X, Zhu Y, Jiang T, Guo X, Qin Y, Sha J Nature. 2022 Dec;612(7941):725-731. doi: 10.1038/s41586-022-05508-0. Epub 2022 , Dec 14. PMID:36517592[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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