Identification of the major tRNAPhe binding domain in the tetrameric structure of cytoplasmic phenylalanyl‐tRNA synthetase from baker's yeast

FEBS Letters

Fasiolo, F.¹  Boulanger, Y.¹  Ebel, J.P.¹  Potier, S.¹  Sanni, A.¹ 

[1] Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 Rue Descartes, 67084 Strasbourg Cedex, France

关键词: Phenylalanyl-tRNA synthetase;    tRNAPhe-binding domain;   

DOI  :  10.1016/0014-5793(89)80500-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Native cytoplasmic phenylalanyl-tRNA synthetase from baker's yeast is a tetramer of the α₂β₂ type. On mild tryptic cleavage it gives rise to a modified ∡₂β′₂ form that has lost the tRNA^Phe binding capacity but is still able to activate phenylalanine. In this paper are presented data concerning peptides released by this limited proteolytic conversion as well as those arising from exhaustive tryptic digestion of the truncated β′ subunit. Each purified peptide was unambiguously assigned to a unique stretch of the β subunit amino acid sequence that was recently determined via gene cloning and DNA sequencing. Together with earlier results from affinity labelling studies the present data show that the Lys 172—Ile 173 bond is the unique target of trypsin under mild conditions and that the N-terminal domain of each β subunit (residues 1–172) contains the major tRNA^Phe binding sites.

【 授权许可】

Unknown