High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome

Yaser Hashem, Amedee des Georges, Jie Fu, Sarah N. Buss, Fabrice Jossinet, Amy Jobe, Qin Zhang, Hstau Y. Liao, Robert A. Grassucci, Chandrajit Bajaj, Eric Westhof, Susan Madison-Antenucci and Joachim Frank ()
Additional contact information
Yaser Hashem: Howard Hughes Medical Institute (HHMI), Columbia University
Amedee des Georges: Howard Hughes Medical Institute (HHMI), Columbia University
Jie Fu: Columbia University
Sarah N. Buss: Wadsworth Center
Fabrice Jossinet: Architecture et Réactivité de l’ARN, Université de Strasbourg, Institut de Biologie Moléculaire et Cellulaire (CNRS)
Amy Jobe: Columbia University
Qin Zhang: Institute for Computational Engineering and Sciences, University of Texas
Hstau Y. Liao: Columbia University
Robert A. Grassucci: Howard Hughes Medical Institute (HHMI), Columbia University
Chandrajit Bajaj: Institute for Computational Engineering and Sciences, University of Texas
Eric Westhof: Architecture et Réactivité de l’ARN, Université de Strasbourg, Institut de Biologie Moléculaire et Cellulaire (CNRS)
Susan Madison-Antenucci: Wadsworth Center
Joachim Frank: Howard Hughes Medical Institute (HHMI), Columbia University

Nature, 2013, vol. 494, issue 7437, 385-389

Abstract: High-resolution cryo-electron microscopy shows that the Trypanosoma brucei kinetoplastid ribosome is characterized by the presence of large expansion segments, ribosomal-protein extensions and additional rRNA insertions, which may have implications for the protein-translation regulation process.

Date: 2013
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DOI: 10.1038/nature11872

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