tRNAPhe deprived of 3′‐terminal adenosyl residue does not stimulate adenosine aminoacylation catalysed by phenylalanyl‐tRNA synthetase from Escherichia coli

FEBS Letters

Boutorin, A.S.¹  Lavrik, O.I.¹  Gordienko, V.A.¹  Moor, N.A.¹ 

[1] Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of the USSR Academy of Sciences, Novosibirsk 630090, USSR

关键词: Phenylalanyl-tRNA synthetase;    Aminoacyladenosine;    Aminoacylation;    Dithiothreitol;    tRNA;    Ado;    adenosine;    DTT;    dithiothreitol;    tRNAPhe;    phenylalanyl-specific tRNA;    tRNAPhe −A;    tRNAPhe deprived of 3′-terminal adenosyl residue;    PRS;    phenylalanyl-tRNA synthetase;   

DOI  :  10.1016/0014-5793(88)80258-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phenylalanyl-tRNA synthetase from Escherichia coli does not catalyze the [¹⁴C]phenylalanyl residue transfer from phenylalanyl-adenylate to adenosine either in the presence or absence of homologous tRNA^Phe and tRNA^Phe _−A. When the reaction mixture contained dithiothreitol, radioactive substance was detected having a mobility on HPLC column close to that of aminoacyladenosine. The amount of this product depended on the concentration of dithiothreitol in the mixture. Phenylalanyl residue was suggested to undergo transfer from aminoacyladenylate to dithiothreitol molecule.

【 授权许可】

Unknown