Structural insights into the evolution of late steps of translation initiation in the three domains of life

Kazan, Ramy; Bourgeois, Gabrielle; Lazennec‐Schurdevin, Christine; Coureux, Pierre‐Damien; Mechulam, Yves; Schmitt, Emmanuelle

doi:10.1016/j.biochi.2023.02.002

Cited by 4 publications

(5 citation statements)

References 93 publications

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“…The path of model-SD mRNA towards the exit channel corresponds to that observed in P. abyssi IC 41,56 . In the mRNA exit chamber, the Shine-Dalgarno sequence of the mRNA is base-paired with the 3'end of the 16S rRNA (Figure 6A).…”

Section: Initiation Complex With An Sd-containing Mrnamentioning

confidence: 64%

“…Interestingly, the number of rRNA modifications is much less than that in the SSU of the two Thermococcales P. abyssi and T. kodakarensis 41,56,59 (Supplementary Table 3). In particular only four N4-acetylcytidines were identified.…”

Section: Specificities Of S Solfataricus Small Ribosomal Subunitmentioning

confidence: 99%

“…Archaeal translation initiation has both bacterial and eukaryotic features [40][41][42][43] . Archaeal initiation factors, aIF1, aIF1A, aIF2, and aIF5B correspond to a subset of eukaryotic translation initiation factors.…”

Section: Introductionmentioning

confidence: 99%

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Cryo-EM Structures ofSaccharolobus solfataricusInitiation Complexes with Leaderless mRNAs Highlight Archaeal Features and Eukaryotic Proximity

Bourgeois,

Coureux,

Lazennec-Schurdevin

et al. 2024

Preprint

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The archaeal ribosome is of the eukaryotic type. Genomic and phylogenetic studies have indicated that TACK and Asgard, the closest relatives of eukaryotes, have ribosomes containing eukaryotic ribosomal proteins not found in other archaeal branches, eS25, eS26 and eS30. In our study, we investigated the case ofSaccharolobus solfataricus, a crenarchaeon belonging to the TACK branch, which mainly uses leaderless mRNAs. We characterized the small ribosomal subunit ofS. solfataricusbound to SD-leadered or leaderless mRNAs (lmRNAs). Cryo-EM structures show for the first time archaeal versions of eS25, eS26 and eS30 proteins bound to the small subunit. In addition, we identify two novel ribosomal proteins named aS33 and aS34 as well as a domain of eS6, that highlight the diversity of archaeal ribosomes. Leaderless mRNAs are bound to the small ribosomal subunit, and the 5’-triphosphate group contributes to their binding. Archaeal eS26 is in the mRNA exit channel wrapped around the 3’ end of ribosomal RNA, as it is in eukaryotes. Its position is not compatible with an SD:antiSD duplex in the mRNA exit channel. Overall, our results suggest a role of eS26 in translation regulation and possible evolutionary routes from archaeal to eukaryotic translation.

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Section: Initiation Complex With An Sd-containing Mrnamentioning

confidence: 64%

Section: Specificities Of S Solfataricus Small Ribosomal Subunitmentioning

confidence: 99%

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Cryo-EM Structures ofSaccharolobus solfataricusInitiation Complexes with Leaderless mRNAs Highlight Archaeal Features and Eukaryotic Proximity

Bourgeois,

Coureux,

Lazennec-Schurdevin

et al. 2024

Preprint

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“…Insights into the mechanism of tRNA stabilization in the ribosome lead to an understanding of the evolution of the molecular mechanisms of protein synthesis. 11 Since proteins play a major role in cellular functions, translation is an important process in cells. To understand the translation in detail, the three-dimensional structures of ribosomes have been elucidated.…”

Section: Toc Graphicmentioning

confidence: 99%

Stabilization Mechanism of Initiator Transfer RNA in the Small Ribosomal Subunit from Coarse-Grained Molecular Simulations

Mori,

Tanaka

2024

Preprint

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Proteins play a variety of roles in biological phenomena in cells. Proteins are synthesized by a ribosome, which is a large molecular complex composed of proteins and nucleic acids. Among many molecules involved in the process of protein synthesis, transfer RNA (tRNA) is one of the essential molecules. In this study, coarse-grained molecular dynamics simulations were performed to understand how the tRNA molecule is stabilized in the ribosome, and the free energy along the dissociation path of the tRNA was calculated. We found that some ribosomal proteins, which are components of the ribosome, are involved in the stabilization of the tRNA. The positively charged amino acid residues in the C-terminal region of the ribosomal proteins are particularly important for the stabilization. These findings contribute to our understanding of the molecular evolution of protein synthesis in terms of the ribosome, which is a universal component of life.TOC Graphic

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“…Once the start codon has been found, eIF2 is released from the PIC in its GDP-bound form. Final steps of translation initiation allow the recruitment of the large ribosomal subunit and the formation of a ribosome competent for elongation (Kazan et al, 2023). Specific binding of the initiator tRNA to eIF2-GTP and the control of the nucleotide state of the factor are crucial for efficient translation initiation (Dubiez et al, 2015;Hinnebusch, 2014).…”

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confidence: 99%

Binding of human Cdc123 to eIF2γ

Peralta

Vandroux

Neumann-Arnold

et al. 2023

Journal of Structural Biology

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Structural insights into the evolution of late steps of translation initiation in the three domains of life

Cited by 4 publications

References 93 publications

Cryo-EM Structures ofSaccharolobus solfataricusInitiation Complexes with Leaderless mRNAs Highlight Archaeal Features and Eukaryotic Proximity

Cryo-EM Structures ofSaccharolobus solfataricusInitiation Complexes with Leaderless mRNAs Highlight Archaeal Features and Eukaryotic Proximity

Stabilization Mechanism of Initiator Transfer RNA in the Small Ribosomal Subunit from Coarse-Grained Molecular Simulations

Binding of human Cdc123 to eIF2γ

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