Interaction of methionine-specific tRNAs from Escherichia coli with immobilized elongation factor Tu.
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.
D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism; D008715:Methionine / Q000378:metabolism*; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012358:RNA, Transfer, Met; D013329:Structure-Activity Relationship
D012346:RNA, Transfer, Amino Acyl; D012358:RNA, Transfer, Met; C026464:tRNA(m)(Met), methionine-; C024988:tRNA, formylmethionine-; D006160:Guanosine Triphosphate; D008715:Methionine; D010444:Peptide Elongation Factor Tu