Premium
Interaction of methionine‐specific tRNAs from Escherichia coli with immobilized elongation factor Tu
Author(s) -
Fischer W.,
Doi T.,
Ikehara M.,
Ohtsuka E.,
Sprinzl M.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80062-4
Subject(s) - ef tu , gtp' , transfer rna , ternary complex , elongation factor , escherichia coli , nucleotide , base pair , biochemistry , chemistry , aminoacyl trna , stereochemistry , biology , rna , dna , enzyme , ribosome , gene
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 C 1 ‐G 72 base pair binds much more strongly to immobilized EF‐Tu·GTP than the native aminoacyl(aa)‐tRNA with non‐base‐paired C 1 A 72 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.