Interaction of fMet-tRNAfMet, Met-tRNAfMet, and Met-tRNAmMet with bacterial elongation factor Tu:GTP complex: discrimination against fMet-tRNAfMet.
Dissociation constant of aminoacyl-tRNA:EF-Tu:GTP complex into aminoacyl-tRNA and EF-Tu:GTP was estimated by the RNase-resistance assay developed by us. The experimental results showed that EF-Tu:GTP has a high affinity for Met-tRNAfMet (E. coli) and Met-tRNAmMet, but not fMet-tRNAfMet. The process of the formylation for Metm-tRNAfMet may provide a security against incorrect translation at GUG (valine) and UUG (leucine) codons in the elongation step.
D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism*; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012358:RNA, Transfer, Met; D013329:Structure-Activity Relationship
D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; D012358:RNA, Transfer, Met; C026464:tRNA(m)(Met), methionine-; C024988:tRNA, formylmethionine-; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu