Interaction of methionine‐specific tRNAs from Escherichia coli with immobilized elongation factor Tu

FEBS Letters

Doi, T.¹  Ikehara, M.¹  Fischer, W.²  Ohtsuka, E.¹  Sprinzl, M.² 

[1] Faculty of Pharmaceutical Sciences, Osaka University, Suita 565, Japan;Lehrstuhl für Biochemie, Universität Bayreuth, Postfach 30 08, D-8580 Bayreuth, FRG

关键词: Protein biosynthesis;    Initiator tRNA;    Elongation factor Tu;    Modified tRNA;    Affinity chromatography;    Protein-nucleic acid interaction;    EF-Tu;    elongation factor Tu;    aa-tRNA;    aminoacyl-tRNA;   

DOI  :  10.1016/0014-5793(85)80062-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interaction of three different Met-tRNAs^Met from E. coli with bacterial elongation factor (EF) Tu · GTP was investigated by affinity chromatography. Met-tRNA^fMet which lacks the base pair at the end of the acceptor stem binds only weakly to EF-Tu·GTP, while Met-tRNA^mMet has a high affinity for the elongation factor. A modified Met-tRNA^fMet which has a C₁-G₇₂ base pair binds much more strongly to immobilized EF-Tu·GTP than the native aminoacyl(aa)-tRNA with non-base-paired C₁A₇₂ at this position, demonstrating that the base pair including the first nucleotide in the tRNA is one of the essential structural requirements for the aa-tRNA·EF-Tu·GTP ternary complex formation.

【 授权许可】

Unknown