Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (76K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (10)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Szymanski, M.
Right arrow Articles by Barciszewski, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Szymanski, M.
Right arrow Articles by Barciszewski, J.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2001, Vol. 29, No. 1 288-290
© 2001 Oxford University Press

Aminoacyl-tRNA synthetases database

Maciej Szymanski, Marzanna A. Deniziak and Jan Barciszewski*

Institute of Bioorganic Chemistry of the Polish Academy of Sciences, Noskowskiego 12/14, 61-704 Poznan, Poland

Aminoacyl-tRNA synthetases (AARSs) are at the center of the question of the origin of life. They constitute a family of enzymes integrating the two levels of cellular organization: nucleic acids and proteins. AARSs arose early in evolution and are believed to be a group of ancient proteins. They are responsible for attaching amino acid residues to their cognate tRNA molecules, which is the first step in the protein synthesis. The role they play in a living cell is essential for the precise deciphering of the genetic code. The analysis of AARSs evolutionary history was not possible for a long time due to a lack of a sufficiently large number of their amino acid sequences. The emerging picture of synthetases’ evolution is a result of recent achievements in genomics [Woese,C., Olsen,G.J., Ibba,M. and Söll,D. (2000) Microbiol. Mol. Biol. Rev., 64, 202–236]. In this paper we present a short introduction to the AARSs database. The updated database contains 1047 AARS primary structures from archaebacteria, eubacteria, mitochondria, chloroplasts and eukaryotic cells. It is the compilation of amino acid sequences of all AARSs known to date, which are available as separate entries via the WWW at http://biobases.ibch.poznan.pl/aars/ .

* To whom correspondence should be addressed. Tel: +48 61 852 8503; Fax: +48 61 852 0532; Email: jbarcisz{at}ibch.poznan.pl


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Nucleic Acids ResHome page
L.-T. Guo, X.-L. Chen, B.-T. Zhao, Y. Shi, W. Li, H. Xue, and Y.-X. Jin
Human tryptophanyl-tRNA synthetase is switched to a tRNA-dependent mode for tryptophan activation by mutations at V85 and I311
Nucleic Acids Res., September 27, 2007; 35(17): 5934 - 5943.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Jia, X.-L. Chen, L.-T. Guo, Y.-D. Yu, J.-P. Ding, and Y.-X. Jin
Residues Lys-149 and Glu-153 Switch the Aminoacylation of tRNATrp in Bacillus subtilis
J. Biol. Chem., October 1, 2004; 279(40): 41960 - 41965.
[Abstract] [Full Text] [PDF]


Home page
Antimicrob. Agents Chemother.Home page
D. Beyer, H.-P. Kroll, R. Endermann, G. Schiffer, S. Siegel, M. Bauser, J. Pohlmann, M. Brands, K. Ziegelbauer, D. Haebich, et al.
New Class of Bacterial Phenylalanyl-tRNA Synthetase Inhibitors with High Potency and Broad-Spectrum Activity
Antimicrob. Agents Chemother., February 1, 2004; 48(2): 525 - 532.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
F. Xu, X. Chen, L. Xin, L. Chen, Y. Jin, and D. Wang
Species-specific differences in the operational RNA code for aminoacylation of tRNATrp
Nucleic Acids Res., October 15, 2001; 29(20): 4125 - 4133.
[Abstract] [Full Text] [PDF]



Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.