Crystal Structure of the Eukaryotic 60S Ribosomal Subunit in Complex with Initiation Factor 6

  title={Crystal Structure of the Eukaryotic 60S Ribosomal Subunit in Complex with Initiation Factor 6},
  author={Sebastian Klinge and Felix Voigts-Hoffmann and Marc Leibundgut and Sofia Arpagaus and Nenad Ban},
  pages={941 - 948}
The 3.5 angstrom–resolution structure provides insights into the architecture of the eukaryotic ribosome and its regulation. Protein synthesis in all organisms is catalyzed by ribosomes. In comparison to their prokaryotic counterparts, eukaryotic ribosomes are considerably larger and are subject to more complex regulation. The large ribosomal subunit (60S) catalyzes peptide bond formation and contains the nascent polypeptide exit tunnel. We present the structure of the 60S ribosomal subunit… 

Crystal structure of eukaryotic ribosome and its complexes with inhibitors

  • G. YusupovaM. Yusupov
  • Biology, Chemistry
    Philosophical Transactions of the Royal Society B: Biological Sciences
  • 2017
The crystal structure of the entire 80S ribosome from yeast is discussed, which reveals its eukaryotic-specific features, and application of X-ray crystallography of the 80S Ribosome for investigation of the binding mode for distinct compounds known to inhibit or modulate the protein-translation function of the ribosomes is referred to.

Extensions, Extra Factors, and Extreme Complexity: Ribosomal Structures Provide Insights into Eukaryotic Translation.

This review highlights the past decade's structural work on eukaryotic ribosomes and its implications on the understanding of eUKaryotic translation.

Assembly of the small ribosomal subunit in yeast: mechanism and regulation.

This review aims to integrate new results from cryo-electron microscopy, X-ray crystallography, and other biochemical and molecular biology methods into an updated view of small sub unit biogenesis and its regulation, in yeast, from transcription to the formation of the mature small subunit.

Mechanistic insight into eukaryotic 60S ribosomal subunit biogenesis by cryo-electron microscopy.

Cryo-electron microscopy of natively purified pre-60S particles and in vitro reconstituted ribosome assembly factor complexes provide detailed insights into the assembly and maturation of the central protuberance of the 60S subunit, the network of biogenesis factors near the ribosomal tunnel exit, and the functional activation of the large Ribosomal subunit during cytoplasmic maturation.

Evolution and assembly of the ribosome

The complex history presented for “core” protein S4 suggests the existence of a gene pool before the emergence of bacterial lineages and reflects the pervasive nature of HGT in subsequent bacterial evolution, and is proven to be stable throughout the micro-second molecular dynamics simulations.

Molecular Architecture of a Eukaryotic Translational Initiation Complex

The use of recent advances in cryo-EM to determine a relatively high-resolution structure of the eIF5B-ribosome complex from a very small fraction of a sample could be a general approach for the study of other dynamic or transient biological complexes.

Eukaryotic protein uS19: a component of the decoding site of ribosomes and a player in human diseases.

Current available data on the involvement of rp uS19 in the operation of the translational machinery and in the maturation of 40S subunits are reviewed, on its extra-ribosomal function, and on relationships between mutations in the RPS15 gene and certain human diseases are reviewed.



Crystal Structure of the Eukaryotic 40S Ribosomal Subunit in Complex with Initiation Factor 1

The structure provides insight into how protein synthesis is initiated and into the evolution of the eukaryotic ribosome, including the function of eIF1 as well as signaling and regulation mediated by the ribosomal proteins RACK1 and rpS6e.

Crystal Structure of the Eukaryotic Ribosome

The crystal structure of the yeast 80S ribosome determined at 4.15 angstrom resolution reveals the higher complexity of eukaryotic ribosomes, which are 40% larger than their bacterial counterparts.

Localization of eukaryote-specific ribosomal proteins in a 5.5-Å cryo-EM map of the 80S eukaryotic ribosome

Near-complete atomic models of the 80S ribosome provide insights into the structure, function, and evolution of the eukaryotic translational apparatus.

The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.

The crystal structure of the large ribosomal subunit from Haloarcula marismortui is determined at 2.4 angstrom resolution, and it includes 2833 of the subunit's 3045 nucleotides and 27 of its 31 proteins.

Crystal structures of ribosome anti-association factor IF6

Comparative protein structure modeling with other known archaeal and eukaryotic homologs demonstrated the presence of two conserved surface regions, one or both of which may bind the large ribosomal subunit.

Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-Å resolution

Accurate assignment of the rRNA expansion segments (ES) and variable regions has revealed unique ES–ES and r-protein–ES interactions, providing insight into the structure and evolution of the eukaryotic ribosome.

Powering through ribosome assembly.

Ribosome assembly factors such as ATPases, GTPases, and kinases hydrolyze nucleotide triphosphates are reviewed and roles of energy-releasing enzymes in the assembly process are proposed to explain why energy is used for a process that occurs largely spontaneously in bacteria.