Literature DB >> 10592262

Aminoacyl-tRNA synthetases database Y2K.

M Szymanski1, J Barciszewski.   

Abstract

The aminoacyl-tRNA synthetases (AARS) are a diverse group of enzymes that ensure the fidelity of transfer of genetic information from DNA into protein. They catalyse the attachment of amino acids to transfer RNAs and thereby establish the rules of the genetic code by virtue of matching the nucleotide triplet of the anticodon with its cognate amino acid. Currently, 818 AARS primary structures have been reported from archaebacteria, eubacteria, mitochondria, chloro-plasts and eukaryotic cells. The database is a compilation of the amino acid sequences of all AARSs, known to date, which are available as separate entries or alignments of related proteins via the WWW at http://rose.man.poznan.pl/aars/index.html

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Year:  2000        PMID: 10592262      PMCID: PMC102446          DOI: 10.1093/nar/28.1.326

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


  32 in total

1.  Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events.

Authors:  Y I Wolf; L Aravind; N V Grishin; E V Koonin
Journal:  Genome Res       Date:  1999-08       Impact factor: 9.043

Review 2.  Aminoacyl-tRNA synthetases: a new image for a classical family.

Authors:  S A Martinis; P Plateau; J Cavarelli; C Florentz
Journal:  Biochimie       Date:  1999-07       Impact factor: 4.079

Review 3.  RNA-protein complexes.

Authors:  S Cusack
Journal:  Curr Opin Struct Biol       Date:  1999-02       Impact factor: 6.809

4.  Aminoacyl-tRNA synthetases: a family of expanding functions. Mittelwihr, France, October 10-15, 1999.

Authors:  S A Martinis; P Plateau; J Cavarelli; C Florentz
Journal:  EMBO J       Date:  1999-09-01       Impact factor: 11.598

Review 5.  Histidyl-tRNA synthetase.

Authors:  W Freist; J F Verhey; A Rühlmann; D H Gauss; J G Arnez
Journal:  Biol Chem       Date:  1999-06       Impact factor: 3.915

Review 6.  Archaeal aminoacyl-tRNA synthesis: diversity replaces dogma.

Authors:  D Tumbula; U C Vothknecht; H S Kim; M Ibba; B Min; T Li; J Pelaschier; C Stathopoulos; H Becker; D Söll
Journal:  Genetics       Date:  1999-08       Impact factor: 4.562

7.  Enzyme structure with two catalytic sites for double-sieve selection of substrate.

Authors:  O Nureki; D G Vassylyev; M Tateno; A Shimada; T Nakama; S Fukai; M Konno; T L Hendrickson; P Schimmel; S Yokoyama
Journal:  Science       Date:  1998-04-24       Impact factor: 47.728

8.  The accessory subunit of mtDNA polymerase shares structural homology with aminoacyl-tRNA synthetases: implications for a dual role as a primer recognition factor and processivity clamp.

Authors:  L Fan; P C Sanschagrin; L S Kaguni; L A Kuhn
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-17       Impact factor: 11.205

9.  Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin.

Authors:  L F Silvian; J Wang; T A Steitz
Journal:  Science       Date:  1999-08-13       Impact factor: 47.728

10.  Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen.

Authors:  M Beaulande; N Tarbouriech; M Härtlein
Journal:  Nucleic Acids Res       Date:  1998-01-15       Impact factor: 16.971

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  2 in total

1.  Specific induction of Z-DNA conformation by a nuclear localization signal peptide of lupin glutaminyl tRNA synthetase.

Authors:  A Krzyzaniak; M Siatecka; A Szyk; P Mucha; P Rekowski; G Kupryszewski; J Barciszewski
Journal:  Mol Biol Rep       Date:  2000-03       Impact factor: 2.316

2.  Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains.

Authors:  Xiang-Lei Yang; Francella J Otero; Robert J Skene; Duncan E McRee; Paul Schimmel; Llúis Ribas de Pouplana
Journal:  Proc Natl Acad Sci U S A       Date:  2003-12-11       Impact factor: 11.205

  2 in total

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