Literature DB >> 17150540

Determination of tryptophan tRNA recognition sites for tryptophanyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1.

Wataru Tsuchiya1, Takuya Umehara, Atsushi Kuno, Tsunemi Hasegawa.   

Abstract

To investigate the recognition mechanism of tryptophan tRNA by tryptophanyl-tRNA synthetase from extreme hyperthermophilic and aerobic archaeon, Aeropyrum pernix K1, tryptophanylation activities were examined by using mutant tryptophan tRNA transcripts prepared by in vitro transcription system. Their transcripts were aminoacylated with tryptophan by overexpressed A. pernix tryptophanyl-tRNA synthetase. The results indicated that anticodon nucleotides C34, C35 and A36, discriminator base A73, G1-C72 and G2-C71 base pairs of acceptor stem were base-specifically recognized by A. pernix tryptophanyl-tRNA synthetase.

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Year:  2004        PMID： 17150540     DOI： 10.1093/nass/48.1.185

Source DB:  PubMed          Journal:  Nucleic Acids Symp Ser (Oxf)        ISSN： 0261-3166


  3 in total

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Journal:  J Bacteriol       Date:  2008-08-29       Impact factor: 3.490

2.  Identifying the ligated amino acid of archaeal tRNAs based on positions outside the anticodon.

Authors:  Tal Galili; Hila Gingold; Shaul Shaul; Yoav Benjamini
Journal:  RNA       Date:  2016-08-11       Impact factor: 4.942

3.  Mapping hidden potential identity elements by computing the average discriminating power of individual tRNA positions.

Authors:  Aron Szenes; Gábor Pál
Journal:  DNA Res       Date:  2012-02-28       Impact factor: 4.458
  3 in total

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