Conserved amino acids near the carboxy terminus of bacterial tyrosyl-tRNA synthetase are involved in tRNA and Tyr-AMP binding

Salazar, JC; Zúñiga R.; Lefimil C; Soll, D; Orellana O.

Abstract

Bacterial tyrosyl-tRNA synthetases occur in two large subfamilies, TyrRS and TyrRZ, that possess about 25% amino acid identity. Their amino-terminal region, the active site domain, is more conserved (>36% identity). The carboxy-terminal segment of these enzymes includes the tRNA binding domain and contains only few conserved residues. Replacement of three of these residues in Acidithiobacillus ferrooxidans TyrRZ revealed that S356 and K395 play roles in tRNA binding, while H306, a residue at the junction of the catalytic and tRNA binding domains, stabilizes the Tyr-AMP:TyrRZ complex. The replacement data suggest that conserved amino acids in A. ferrooxidans TyrRZ and Bacillus stearothermophilus TyrRS play equivalent roles in enzyme function. © 2001 Federation of European Biochemical Societies.

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Título según WOS: Conserved amino acids near the carboxy terminus of bacterial tyrosyl-tRNA synthetase are involved in tRNA and Tyr-AMP binding
Título según SCOPUS: Conserved amino acids near the carboxy terminus of bacterial tyrosyl-tRNA synthetase are involved in tRNA and Tyr-AMP binding
Título de la Revista: FEBS LETTERS
Volumen: 491
Asunto: 3
Editorial: ELSEVIER SCIENCE BV
Fecha de publicación: 2001-01-01
Página de inicio: 257
Página final: 260
Idioma: English
DOI/URL:

10.1016/S0014-5793(01)02214-1

Identificador: 10.1016/S0014-5793(01)02214-1
Notas: ISI, SCOPUS