Effect of elongation factor Tu on the conformation of phenylalanyl-tRNAPhe.
Structural features of the tRNAPhe molecule upon ternary complex formation with the bacterial elongation factor Tu were investigated. Phosphodiester bonds at positions 18 and 34 were found to be labilized in bound tRNA. Conversely, a higher stability of the phosphodiester links at positions 20, 21 and 36 was detected. Using ethylnitrosourea as a chemical probe a conformational change occurring at phosphate position 53 was observed in complexed tRNA. These results are interpreted by a structural rearrangement of the nucleic acid induced by complex formation.
D055598:Chemical Phenomena; D002621:Chemistry; D005038:Ethylnitrosourea; D006160:Guanosine Triphosphate; D009690:Nucleic Acid Conformation; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl
D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; C037801:tRNA, phenylalanylphenylalanine-; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu; D005038:Ethylnitrosourea