Loading…

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

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...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2010-11, Vol.107 (46), p.19754-19759
Main Authors: Armache, Jean-Paul, Jarasch, Alexander, Anger, Andreas M, Villa, Elizabeth, Becker, Thomas, Bhushan, Shashi, Jossinet, Fabrice, Habeck, Michael, Dindar, Gülcin, Franckenberg, Sibylle, Marquez, Viter, Mielke, Thorsten, Thomm, Michael, Berninghausen, Otto, Beatrix, Birgitta, Söding, Johannes, Westhof, Eric, Wilson, Daniel N, Beckmann, Roland
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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-Å resolution, together with a 6.1-Å 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1010005107