Structure of the 70S ribosome from human pathogen Staphylococcus aureus.
Fiche publication
Date publication
décembre 2016
Journal
Nucleic acids research
Auteurs
Membres identifiés du Cancéropôle Est :
Dr ROMBY Pascale, Dr YUSUPOV Marat, Dr YUSUPOVA Gulnara
Tous les auteurs :
Khusainov I, Vicens Q, Bochler A, Grosse F, Myasnikov A, Ménétret JF, Chicher J, Marzi S, Romby P, Yusupova G, Yusupov M, Hashem Y
Lien Pubmed
Résumé
Comparative structural studies of ribosomes from various organisms keep offering exciting insights on how species-specific or environment-related structural features of ribosomes may impact translation specificity and its regulation. Although the importance of such features may be less obvious within more closely related organisms, their existence could account for vital yet species-specific mechanisms of translation regulation that would involve stalling, cell survival and antibiotic resistance. Here, we present the first full 70S ribosome structure from Staphylococcus aureus, a Gram-positive pathogenic bacterium, solved by cryo-electron microscopy. Comparative analysis with other known bacterial ribosomes pinpoints several unique features specific to S. aureus around a conserved core, at both the protein and the RNA levels. Our work provides the structural basis for the many studies aiming at understanding translation regulation in S. aureus and for designing drugs against this often multi-resistant pathogen.
Mots clés
Amino Acid Sequence, Bacillus subtilis, chemistry, Bacterial Proteins, chemistry, Binding Sites, Cryoelectron Microscopy, Escherichia coli, chemistry, Gene Expression, Molecular Dynamics Simulation, Nucleic Acid Conformation, Protein Binding, Protein Biosynthesis, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, RNA, Bacterial, chemistry, Ribosomal Proteins, chemistry, Ribosomes, chemistry, Sequence Alignment, Sequence Homology, Amino Acid, Species Specificity, Staphylococcus aureus, chemistry, Thermus thermophilus, chemistry
Référence
Nucleic Acids Res.. 2016 12 1;44(21):10491-10504