Contributors: Laboratoire de Biologie Structurale de la Cellule (BIOC); École polytechnique (X); Institut Polytechnique de Paris (IP Paris)-Institut Polytechnique de Paris (IP Paris)-Centre National de la Recherche Scientifique (CNRS); Microbiologie moléculaire et biochimie structurale - Molecular Microbiology and Structural Biochemistry (MMSB); Université Claude Bernard Lyon 1 (UCBL); Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS); Spectrométrie de Masse pour la Biologie – Mass Spectrometry for Biology (UTechS MSBio); Institut Pasteur [Paris] (IP)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité); Laboratoire de Chimie Moléculaire (LCM); This work was supported by grants from the Centre National de la Recherche Scientifique and Ecole polytechnique to Unité Mixte de Recherche n°7654, by a grant from the Agence Nationale de la Recherche (ANR-17-CE11–0037; TREMTI) and served as preliminary results for grant ANR-24-CE11-4225 (LmRNA). Cryo-EM data benefited from access to CM01 beamline (ESRF, Grenoble), the Nanoimaging facility (Institut Pasteur, Paris, created with the help of ANR-11-EQPX-008 grant) and the Interdisciplinary Center for Electron Microscopy of Ecole Polytechnique (CIMEX).; We thank the staff at these facilities, and in particular Isai Kandiah and Daouda Traore (ESRF), Stéphane Tachon (Institut Pasteur), Eric Larquet and Kassiogé Dembélé (CIMEX). We thank David Mignon for skillful computer assistance, Michel Fromant for the gift of S. solfataricus cells and Antoine Mechulam for writing useful computer scripts. We thank Sebastien Ferreira-Cerca for helpful discussions.; ANR-17-CE11-0037,TREMTI,Etude du démarrage de la traduction par cryo-microscopie électronique résolue en temps(2017); ANR-24-CE11-4225,LmRNA,Démarrage de la traduction avec des ARN messagers sans leaders(2024); ANR-11-EQPX-0008,CACSICE,Centre d'analyse de systèmes complexes dans les environnements complexes(2011)
نبذة مختصرة : The archaeal ribosome is of the eukaryotic type. TACK and Asgard superphyla, the closest relatives of eukaryotes, have ribosomes containing eukaryotic ribosomal proteins not found in other archaea, eS25, eS26 and eS30. Here, we investigate the case of Saccharolobus solfataricus, a TACK crenarchaeon, using mainly leaderless mRNAs. We characterize the small ribosomal subunit of S. solfataricus bound to SD-leadered or leaderless mRNAs. Cryo-EM structures show eS25, eS26 and eS30 bound to the small subunit. We identify two ribosomal proteins, aS33 and aS34, and an additional domain of eS6. Leaderless mRNAs are bound to the small subunit with contribution of their 5’-triphosphate group. Archaeal eS26 binds to the mRNA exit channel wrapped around the 3’ end of rRNA, as in eukaryotes. Its position is not compatible with an SD:antiSD duplex. Our results suggest a positive role of eS26 in leaderless mRNAs translation and possible evolutionary routes from archaeal to eukaryotic translation.
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