Nucleic Acids Research Advance Access originally published online on February 6, 2007
Nucleic Acids Research 2007 35(5):1421-1431; doi:10.1093/nar/gkl1164
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Nucleic Acids Research, 2007, Vol. 35, No. 5 1421-1431
© 2007 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 |
Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation
UPR 9002 ‘Architecture et Reactivité de l'ARN’, Université Louis Pasteur, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15, Rue René Descartes, F-67084 Strasbourg Cedex, France
*To whom correspondence should be addressed. Tel: +33 (0)3 88 41 70 41; Fax: +33 (0)3 88 60 22 18; Email: H.Becker{at}ibmc.u-strasbg.fr Correspondence may also be addressed to Daniel Kern. Tel: +33 (0)3 88 41 70 92; Fax: +33 (0)3 88 60 22 18; Email: D.Kern{at}ibmc.u-strasbg.fr
Received December 20, 2006. Accepted December 20, 2006.
Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein present in various organisms and part of it is present in the C-terminal end of the GatB subunit of GatCAB, a partner of the indirect pathway of Gln-tRNAGln formation. To analyze the peculiarities of the structure–function relationship of this GlnRS related to the Yqey domain, a structure of the protein was solved from crystals diffracting at 2.3 Å and a docking model of the synthetase complexed to tRNAGln constructed. The comparison of the modeled complex with the structure of the E. coli complex reveals that all residues of E. coli GlnRS contacting tRNAGln are conserved in D. radiodurans GlnRS, leaving the functional role of the Yqey domain puzzling. Kinetic investigations and tRNA-binding experiments of full length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved in tRNAGln recognition. They demonstrate that Yqey plays the role of an affinity-enhancer of GlnRS for tRNAGln acting only in cis. However, the presence of Yqey in free state in organisms lacking GlnRS, suggests that this domain may exert additional cellular functions.
The authors wish it to be known that, in their opinion, the first three authors should be regarded as joint First Authors.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  A. Nakamura, K. Sheppard, J. Yamane, M. Yao, D. Soll, and I. Tanaka Two distinct regions in Staphylococcus aureus GatCAB guarantee accurate tRNA recognition Nucleic Acids Res., November 11, 2009; (2009) gkp955v1. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 I. Luque, M. L. Riera-Alberola, A. Andujar, and J. A. G. Ochoa de Alda Intraphylum Diversity and Complex Evolution of Cyanobacterial Aminoacyl-tRNA Synthetases Mol. Biol. Evol., November 1, 2008; 25(11): 2369 - 2389. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Sheppard, J. Yuan, M. J. Hohn, B. Jester, K. M. Devine, and D. Soll From one amino acid to another: tRNA-dependent amino acid biosynthesis Nucleic Acids Res., April 1, 2008; 36(6): 1813 - 1825. [Abstract] [Full Text] [PDF]
|
|