Comparative Study
doi: 10.1016/0014-5793(85)80062-4.
Interaction of methionine-specific tRNAs from Escherichia coli with immobilized elongation factor Tu
- PMID: 3902504
- DOI: 10.1016/0014-5793(85)80062-4
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Comparative Study
Interaction of methionine-specific tRNAs from Escherichia coli with immobilized elongation factor Tu
FEBS Lett.
.
Free article
Abstract
The interaction of three different Met-tRNAsMet from E. coli with bacterial elongation factor (EF) Tu X GTP was investigated by affinity chromatography. Met-tRNAfMet which lacks the base pair at the end of the acceptor stem binds only weakly to EF-Tu X GTP, while Met-tRNAmMet has a high affinity for the elongation factor. A modified Met-tRNAfMet which has a C1-G72 base pair binds much more strongly to immobilized EF-Tu X 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 X EF-Tu X GTP ternary complex formation.
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