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  Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon

Hilal, T., Killam, B. Y., Grozdanović, M., Dobosz-Bartoszek, M., Loerke, J., Bürger, J., et al. (2022). Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon. Science, 376, 1338-1343. doi:10.1126/science.abg38.

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Hilal, Tarek , Author
Killam, Benjamin Y. , Author
Grozdanović, Milica , Author
Dobosz-Bartoszek, Malgorzata, Author
Loerke, Justus , Author
Bürger, Jörg1, Author           
Mielke, Thorsten1, Author           
Copeland, Paul R. , Author
Simonović, Miljan , Author
Spahn, Christian M. T. , Author
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1Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479668              

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 Abstract: The elongation of eukaryotic selenoproteins relies on a poorly understood process of interpreting in-frame UGA stop codons as selenocysteine (Sec). We used cryo-electron microscopy to visualize Sec UGA recoding in mammals. A complex between the noncoding Sec-insertion sequence (SECIS), SECIS-binding protein 2 (SBP2), and 40S ribosomal subunit enables Sec-specific elongation factor eEFSec to deliver Sec. eEFSec and SBP2 do not interact directly but rather deploy their carboxyl-terminal domains to engage with the opposite ends of the SECIS. By using its Lys-rich and carboxyl-terminal segments, the ribosomal protein eS31 simultaneously interacts with Sec-specific transfer RNA (tRNASec) and SBP2, which further stabilizes the assembly. eEFSec is indiscriminate toward l-serine and facilitates its misincorporation at Sec UGA codons. Our results support a fundamentally distinct mechanism of Sec UGA recoding in eukaryotes from that in bacteria.

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Language(s): eng - English
 Dates: 2022-05-102022-06-16
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: DOI: 10.1126/science.abg38
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Title: Science
  Abbreviation : Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: 6 Volume / Issue: 376 Sequence Number: - Start / End Page: 1338 - 1343 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1