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Title | High-Resolution Reconstruction of a C. elegans Ribosome Sheds Light on Evolutionary Dynamics and Tissue Specificity. |
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Journal, issue, pages | RNA, Year 2024 |
Publish date | Aug 29, 2024 |
Authors | Enisha Sehgal / Chloe Wohlenberg / Evan M Soukup / Marcus J Viscardi / Vitor Hugo Balasco Serrão / Joshua A Arribere / |
PubMed Abstract | Caenorhabditis elegans is an important model organism for human health and disease, with foundational contributions to the understanding of gene expression and tissue patterning in animals. An ...Caenorhabditis elegans is an important model organism for human health and disease, with foundational contributions to the understanding of gene expression and tissue patterning in animals. An invaluable tool in modern gene expression research is the presence of a high-resolution ribosome structure, though no such structure exists for C. elegans. Here we present a high-resolution single-particle cryogenic electron microscopy (cryoEM) reconstruction and molecular model of a C. elegans ribosome, revealing a significantly streamlined animal ribosome. Many facets of ribosome structure are conserved in C. elegans, including overall ribosomal architecture and the mechanism of cycloheximide, while other facets such as expansion segments and eL28 are rapidly evolving. We identify uL5 and uL23 as two instances of tissue-specific ribosomal protein paralog expression conserved in Caenorhabditis, suggesting that C. elegans ribosomes vary across tissues. The C. elegans ribosome structure will provide a basis for future structural, biochemical, and genetic studies of translation in this important animal system. |
External links | RNA / PubMed:39209556 |
Methods | EM (single particle) |
Resolution | 2.59 - 2.63 Å |
Structure data | EMDB-44533: High resolution C. elegans 80S ribosome structure EMDB-45392, PDB-9cai: |
Chemicals | ChemComp-SPD: ChemComp-3HE: |
Source |
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Keywords | RIBOSOME / Caenorhabditis elegans / high-resolution single-particle analysis / endogenous purified 80S ribosome |