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Nucleic Acids Research Advance Access originally published online on August 12, 2006
Nucleic Acids Research 2006 34(14):3968-3979; doi:10.1093/nar/gkl560
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Nucleic Acids Research, 2006, Vol. 34, No. 14 3968-3979
© 2006 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes

Hannes Simader, Michael Hothorn, Christine Köhler, Jerome Basquin, George Simos1 and Dietrich Suck*

Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL) Meyerhofstrasse 1, D-69117 Heidelberg, Germany 1 Department of Medicine, University of Thessaly 22 Papakiriazi Street, Larissa, 41222, Greece

*To whom correspondence should be addressed. Tel: 0049 6221 387307; Fax: 0049 6221 387306; Email: suck{at}embl.de

Received May 6, 2006. Revised July 18, 2006. Accepted July 19, 2006.

The yeast aminoacyl-tRNA synthetase (aaRS) complex is formed by the methionyl- and glutamyl-tRNA synthetases (MetRS and GluRS, respectively) and the tRNA aminoacylation cofactor Arc1p. It is considered an evolutionary intermediate between prokaryotic aaRS and the multi- aaRS complex found in higher eukaryotes. While a wealth of structural information is available on the enzymatic domains of single aaRS, insight into complex formation between eukaryotic aaRS and associated protein cofactors is missing. Here we report crystal structures of the binary complexes between the interacting domains of Arc1p and MetRS as well as those of Arc1p and GluRS at resolutions of 2.2 and 2.05 Å, respectively. The data provide a complete structural model for ternary complex formation between the interacting domains of MetRS, GluRS and Arc1p. The structures reveal that all three domains adopt a glutathione S-transferase (GST)-like fold and that simultaneous interaction of Arc1p with GluRS and MetRS is mediated by the use of a novel interface in addition to a classical GST dimerization interaction. The results demonstrate a novel role for this fold as a heteromerization domain specific to eukaryotic aaRS, associated proteins and protein translation elongation factors.


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