Literature DB >> 11125115

Aminoacyl-tRNA synthetases database.

M Szymanski1, M A Deniziak, J Barciszewski.   

Abstract

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/.

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Year:  2001        PMID: 11125115      PMCID: PMC29805          DOI: 10.1093/nar/29.1.288

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN: 0305-1048            Impact factor:   16.971


  30 in total

Review 1.  Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process.

Authors:  C R Woese; G J Olsen; M Ibba; D Söll
Journal:  Microbiol Mol Biol Rev       Date:  2000-03       Impact factor: 11.056

2.  A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases.

Authors:  B Cahuzac; E Berthonneau; N Birlirakis; E Guittet; M Mirande
Journal:  EMBO J       Date:  2000-02-01       Impact factor: 11.598

Review 3.  Transfer RNA recognition by aminoacyl-tRNA synthetases.

Authors:  P J Beuning; K Musier-Forsyth
Journal:  Biopolymers       Date:  1999       Impact factor: 2.505

4.  Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases.

Authors:  L D Sherlin; T L Bullock; K J Newberry; R S Lipman; Y M Hou; B Beijer; B S Sproat; J J Perona
Journal:  J Mol Biol       Date:  2000-06-02       Impact factor: 5.469

5.  Duplication and quadruplication of Arabidopsis thaliana cysteinyl- and asparaginyl-tRNA synthetase genes of organellar origin.

Authors:  N M Peeters; A Chapron; A Giritch; O Grandjean; D Lancelin; T Lhomme; A Vivrel; I Small
Journal:  J Mol Evol       Date:  2000-05       Impact factor: 2.395

6.  The cytokine portion of p43 occupies a central position within the eukaryotic multisynthetase complex.

Authors:  M T Norcum; J A Warrington
Journal:  J Biol Chem       Date:  2000-06-16       Impact factor: 5.157

Review 7.  Footprints of aminoacyl-tRNA synthetases are everywhere.

Authors:  P Schimmel; L Ribas De Pouplana
Journal:  Trends Biochem Sci       Date:  2000-05       Impact factor: 13.807

8.  Perspectives: protein synthesis. Unraveling the riddle of ProCys tRNA synthetase.

Authors:  M Yarus
Journal:  Science       Date:  2000-01-21       Impact factor: 47.728

9.  Synthesis of cysteinyl-tRNA(Cys) by a genome that lacks the normal cysteine-tRNA synthetase.

Authors:  R S Lipman; K R Sowers; Y M Hou
Journal:  Biochemistry       Date:  2000-07-04       Impact factor: 3.162

10.  Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis.

Authors:  Y G Ko; Y S Kang; E K Kim; S G Park; S Kim
Journal:  J Cell Biol       Date:  2000-05-01       Impact factor: 10.539

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  9 in total

1.  Human tryptophanyl-tRNA synthetase is switched to a tRNA-dependent mode for tryptophan activation by mutations at V85 and I311.

Authors:  Li-Tao Guo; Xiang-Long Chen; Bo-Tao Zhao; Yi Shi; Wei Li; Hong Xue; You-Xin Jin
Journal:  Nucleic Acids Res       Date:  2007-08-28       Impact factor: 16.971

2.  Error-prone protein synthesis in parasites with the smallest eukaryotic genome.

Authors:  Sergey V Melnikov; Keith D Rivera; Denis Ostapenko; Arthur Makarenko; Neil D Sanscrainte; James J Becnel; Mark J Solomon; Catherine Texier; Darryl J Pappin; Dieter Söll
Journal:  Proc Natl Acad Sci U S A       Date:  2018-06-18       Impact factor: 11.205

3.  The crystal structures of the α-subunit of the α(2)β (2) tetrameric Glycyl-tRNA synthetase.

Authors:  Kemin Tan; Min Zhou; Rongguang Zhang; Wayne F Anderson; Andrzej Joachimiak
Journal:  J Struct Funct Genomics       Date:  2012-10-06

4.  Species-specific differences in the operational RNA code for aminoacylation of tRNA(Trp).

Authors:  F Xu; X Chen; L Xin; L Chen; Y Jin; D Wang
Journal:  Nucleic Acids Res       Date:  2001-10-15       Impact factor: 16.971

5.  New class of bacterial phenylalanyl-tRNA synthetase inhibitors with high potency and broad-spectrum activity.

Authors:  Dieter Beyer; Hein-Peter Kroll; Rainer Endermann; Guido Schiffer; Stephan Siegel; Marcus Bauser; Jens Pohlmann; Michael Brands; Karl Ziegelbauer; Dieter Haebich; Christine Eymann; Heike Brötz-Oesterhelt
Journal:  Antimicrob Agents Chemother       Date:  2004-02       Impact factor: 5.191

6.  Palindromes in proteins.

Authors:  Malgorzata Giel-Pietraszuk; Marcin Hoffmann; Sylwia Dolecka; Jacek Rychlewski; Jan Barciszewski
Journal:  J Protein Chem       Date:  2003-02

7.  The complex evolutionary history of aminoacyl-tRNA synthetases.

Authors:  Anargyros Chaliotis; Panayotis Vlastaridis; Dimitris Mossialos; Michael Ibba; Hubert D Becker; Constantinos Stathopoulos; Grigorios D Amoutzias
Journal:  Nucleic Acids Res       Date:  2017-02-17       Impact factor: 16.971

8.  A genomic glimpse of aminoacyl-tRNA synthetases in malaria parasite Plasmodium falciparum.

Authors:  Tarun Kumar Bhatt; Charu Kapil; Sameena Khan; Mohamad Aman Jairajpuri; Vinay Sharma; Daniele Santoni; Francesco Silvestrini; Elisabetta Pizzi; Amit Sharma
Journal:  BMC Genomics       Date:  2009-12-31       Impact factor: 3.969

9.  Paths of lateral gene transfer of lysyl-aminoacyl-tRNA synthetases with a unique evolutionary transition stage of prokaryotes coding for class I and II varieties by the same organisms.

Authors:  Shaul Shaul; Ruth Nussinov; Tal Pupko
Journal:  BMC Evol Biol       Date:  2006-03-12       Impact factor: 3.260

  9 in total

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