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  Conformational rearrangements upon start codon recognition in human 48S translation initiation complex

Yi, S.-H., Petrychenko, V., Schliep, J. E., Goyal, A., Linden, A., Chari, A., et al. (2022). Conformational rearrangements upon start codon recognition in human 48S translation initiation complex. Nucleic Acids Research, 50(9), 5282-5298. doi:10.1093/nar/gkac283.

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 Creators:
Yi, S.-H.1, Author           
Petrychenko, V.2, Author           
Schliep, J. E.2, Author           
Goyal, A.1, Author           
Linden, A.3, Author           
Chari, A.4, Author           
Urlaub, H.3, Author           
Stark, H.2, Author           
Rodnina, M. V.1, Author           
Adio, S., Author
Fischer, N.2, Author           
Affiliations:
1Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350156              
2Department of Structural Dynamics, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350272              
3Research Group of Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350290              
4Research Group of Structural Biochemistry and Mechanisms, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350273              

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 Abstract: Selection of the translation start codon is a key step during protein synthesis in human cells. We obtained cryo-EM structures of human 48S initiation complexes and characterized the intermediates of codon recognition by kinetic methods using eIF1A as a reporter. Both approaches capture two distinct ribosome populations formed on an mRNA with a cognate AUG codon in the presence of eIF1, eIF1A, eIF2–GTP–Met-tRNAiMet and eIF3. The ‘open’ 40S subunit conformation differs from the human 48S scanning complex and represents an intermediate preceding the codon recognition step. The ‘closed’ form is similar to reported structures of complexes from yeast and mammals formed upon codon recognition, except for the orientation of eIF1A, which is unique in our structure. Kinetic experiments show how various initiation factors mediate the population distribution of open and closed conformations until 60S subunit docking. Our results provide insights into the timing and structure of human translation initiation intermediates and suggest the differences in the mechanisms of start codon selection between mammals and yeast.

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Language(s): eng - English
 Dates: 2022-04-302022-05-20
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1093/nar/gkac283
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Funding program : SFB860
Funding organization : DFG

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Title: Nucleic Acids Research
Source Genre: Journal
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Pages: - Volume / Issue: 50 (9) Sequence Number: - Start / End Page: 5282 - 5298 Identifier: -