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

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
Source :
Proceedings of the National Academy of Sciences of the United States of America. 11/16/2010, Vol. 107 Issue 46, p19754-19759. 6p. 5 Diagrams.
Publication Year :
2010

Abstract

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 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00278424
Volume :
107
Issue :
46
Database :
Academic Search Index
Journal :
Proceedings of the National Academy of Sciences of the United States of America
Publication Type :
Academic Journal
Accession number :
57412386
Full Text :
https://doi.org/10.1073/pnas.1010005107