Modification of Bacillus subtilis elongation factor Tu by N‐tosyl‐L phenylalanyl chloromethane abolishes its ability to interact with the 3′‐terminal polynucleotide structure but not with the acyl bond in aminoacyl‐tRNA

FEBS Letters

Jonák, Jiří¹  Karas, Karel¹ 

[1] Institute of Molecular Genetics, Czechoslovak Academy of Sciences, Flemingovo n. 2, 166 37 Prague 6, Czechoslovakia

关键词: Elongation factor Tu;    Tosyl-L-phenylalanyl chloromethane;    N-;    EF-Tu-aminoacyl-tRNA interaction;    Aminoacyl-tRNA-binding site;    (Bacillus subtilis);    TPCK;    N-tosyl-L-phenylalanyl chloromethane or L-1-tosylamido-2-phenylethylchloromethyl ketone;    EF-Tu;    elongation factor Tu;   

DOI  :  10.1016/0014-5793(89)81440-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Modification of B. subtilis EF-TU by N-tosyl-L-phenylalanyl chloromethane destroyed its ability to promote protein synthesis and resulted in selective dissociation of the two binding activities of the protein for aminoacyl-tRNA. The modified EF-Tu was completely ineffective in the protection of the 3′-terminal CCA structure of tRNA against pancreatic ribonuclease, while remaining almost fully active in the protection of the ester bond between the 3′-terminal adenosine and the amino acid residue in aminoacyl-tRNA.

【 授权许可】

Unknown