ausblenden:
Schlagwörter:
Cryoelectron Microscopy; Eukaryotic Cells/metabolism/ultrastructure; Evolution, Molecular; Models, Molecular; Protein Transport; RNA, Ribosomal/chemistry/genetics/ultrastructure; Ribosomal Proteins/metabolism/ultrastructure; Ribosomes/metabolism/ultrastructure; Saccharomyces cerevisiae/metabolism/ultrastructure; Species Specificity; Triticum/metabolism
Zusammenfassung:
Protein synthesis in all living organisms occurs on ribonucleoprotein particles, called ribosomes. Despite the universality of this process, eukaryotic ribosomes are significantly larger in size than their bacterial counterparts due in part to the presence of 80 r proteins rather than 54 in bacteria. Using cryoelectron microscopy reconstructions of a translating plant (Triticum aestivum) 80S ribosome at 5.5-A resolution, together with a 6.1-A map of a translating Saccharomyces cerevisiae 80S ribosome, we have localized and modeled 74/80 (92.5%) of the ribosomal proteins, encompassing 12 archaeal/eukaryote-specific small subunit proteins as well as the complete complement of the ribosomal proteins of the eukaryotic large subunit. Near-complete atomic models of the 80S ribosome provide insights into the structure, function, and evolution of the eukaryotic translational apparatus.
