Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases from an extreme thermophile Thermus thermophilus HB8

protein structure and Zn2+ binding

Daisuke Kohda, Shigeyuki Yokoyama, Tatsuo Miyazawa

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases have been purified from an extreme thermophile, Thermus thermophilus HB8. Valyl-tRNA and isoleucyl-tRNA synthetases are found to be monomer proteins (Mr 108000 and 129000, respectively), while methionyl-tRNA synthetase is a dimer protein (Mr 150000). These enzymes are very similar with respect to amino acid compositions and α-helix contents as estimated by circular dichroism analyses. Furthermore, two Zn2+ are tightly bound to each of these synthetases. These data suggest that valyl-tRNA and isoleucyl-tRNA synthetases consist of two domains, each corresponding to the subunit of methionyl-tRNA synthetase.

Original languageEnglish
Pages (from-to)20-23
Number of pages4
JournalFEBS Letters
Volume174
Issue number1
DOIs
Publication statusPublished - Aug 20 1984
Externally publishedYes

Fingerprint

Methionine-tRNA Ligase
Thermus thermophilus
Transfer RNA
Isoleucine-tRNA Ligase
Proteins
Ligases
Circular Dichroism
Dimers
Monomers
Amino Acids
Enzymes
Chemical analysis

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases from an extreme thermophile Thermus thermophilus HB8 : protein structure and Zn2+ binding. / Kohda, Daisuke; Yokoyama, Shigeyuki; Miyazawa, Tatsuo.

In: FEBS Letters, Vol. 174, No. 1, 20.08.1984, p. 20-23.

Research output: Contribution to journalArticle

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