Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 31 March 1995:
Vol. 267. no. 5206, pp. 1958 - 1965
DOI: 10.1126/science.7701318
Prev | Table of Contents | Next

Articles

Science, Vol 267, Issue 5206, 1958-1965
Copyright © 1995 by American Association for the Advancement of Science

articles

Architectures of class-defining and specific domains of glutamyl-tRNA synthetase

O Nureki, DG Vassylyev, K Katayanagi, T Shimizu, S Sekine, T Kigawa, T Miyazawa, S Yokoyama, and K Morikawa

Department of Biophysics and Biochemistry, School of Science, University of Tokyo, Japan.

The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and refined at 2.5 A resolution. The amino-terminal half of GluRS shows a geometrical similarity with that of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) of the same subclass in class I, comprising the class I-specific Rossmann fold domain and the intervening subclass-specific alpha/beta domain. These domains were found to have two GluRS-specific, secondary-structure insertions, which then participated in the specific recognition of the D and acceptor stems of tRNA(Glu) as indicated by mutagenesis analyses based on the docking properties of GluRS and tRNA. In striking contrast to the beta-barrel structure of the GlnRS carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an all-alpha-helix architecture, an alpha-helix cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
From The Cover: An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp.
D. Y. Dubois, M. Blaise, H. D. Becker, V. Campanacci, G. Keith, R. Giege, C. Cambillau, J. Lapointe, and D. Kern (2004)
PNAS 101, 7530-7535
   Abstract »    Full Text »    PDF »
Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases.
R. Banerjee, A. K. Mandal, R. Saha, S. Guha, S. Samaddar, A. Bhattacharyya, and S. Roy (2003)
Nucleic Acids Res. 31, 6035-6042
   Abstract »    Full Text »    PDF »
Genetic, Enzymatic, and Structural Analyses of Phenylalanyl-tRNA Synthetase from Thermococcus kodakaraensis KOD1.
K. Shiraki, M. Tsuji, Y. Hashimoto, K. Fujimoto, S. Fujiwara, M. Takagi, and T. Imanaka (2003)
J. Biochem. 134, 567-574
   Abstract »    Full Text »    PDF »
Structural Basis for Amino Acid and tRNA Recognition by Class I Aminoacyl-tRNA Synthetases.
O. NUREKI, S. FUKAI, S. SEKINE, A. SHIMADA, T. TERADA, T. NAKAMA, M. SHIROUZU, D.G. VASSYLYEV, and S. YOKOYAMA (2001)
Cold Spring Harb Symp Quant Biol 66, 167-174
   Abstract »    PDF »
Aminoacyl-tRNA Synthetases, the Genetic Code, and the Evolutionary Process.
C. R. Woese, G. J. Olsen, M. Ibba, and D. Soll (2000)
Microbiol. Mol. Biol. Rev. 64, 202-236
   Abstract »    Full Text »    PDF »
Cloning of the Glutamyl-tRNA Synthetase (gltX) Gene from Pseudomonas aeruginosa.
C. V. Franklund and J. B. Goldberg (1999)
J. Bacteriol. 181, 3582-3586
   Abstract »    Full Text »
Aminoacylation of tRNA in the evolution of an aminoacyl-tRNA synthetase.
R. S. A. Lipman and Y.-M. Hou (1998)
PNAS 95, 13495-13500
   Abstract »    Full Text »    PDF »
Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis.
A. W. Curnow, D. L. Tumbula, J. T. Pelaschier, B. Min, and D. Soll (1998)
PNAS 95, 12838-12843
   Abstract »    Full Text »    PDF »
The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
W. H. McClain, J. Schneider, S. Bhattacharya, and K. Gabriel (1998)
PNAS 95, 460-465
   Abstract »    Full Text »    PDF »
Identification of Functional Conserved Residues of CTP:glycerol-3-phosphate Cytidylyltransferase. ROLE OF HISTIDINES IN THE CONSERVED HXGH IN CATALYSIS.
Y. S. Park, P. Gee, S. Sanker, E. J. Schurter, E. R. P. Zuiderweg, and C. Kent (1997)
J. Biol. Chem. 272, 15161-15166
   Abstract »    Full Text »    PDF »
Widespread Use of the Glu-tRNAGln Transamidation Pathway among Bacteria. A MEMBER OF THE alpha PURPLE BACTERIA LACKS GLUTAMINYL-tRNA SYNTHETASE.
Y. Gagnon, L. Lacoste, N. Champagne, and J. Lapointe (1996)
J. Biol. Chem. 271, 14856-14863
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)