Aminoacyl-tRNA synthetases from an extreme thermophile, Thermus thermophilus HB8.

D. Kohda, M. Hara, S. Yokoyama, T. Miyazawa

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1 Citation (Scopus)

Abstract

Thermostable aminoacyl-tRNA synthetases specific to Val, Ile, Met and Glu were purified from an extreme thermophile, Thermus thermophilus HB8. As for the subunit compositions and molecular weights, these four aminoacyl-tRNA synthetases are similar to the corresponding enzymes from E. coli and B. stearothermophilus. Val-tRNA, Ile-tRNA and Met-tRNA synthetases from T. thermophilus have two tightly bound zinc ions, whereas Glu-tRNA synthetase does not. The amino acid compositions and secondary structures of Val-tRNA, Ile-tRNA and Met-tRNA synthetases are quite similar to one another. The conformational transition involving the anticodon of E. coli tRNAGlu as complexed with Glu-tRNA synthetase from T. thermophilus is necessary for the aminoacylation activity.

Original languageEnglish
Pages (from-to)153-154
Number of pages2
JournalNucleic acids symposium series
Issue number12
Publication statusPublished - Dec 1 1983
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Medicine(all)

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