Interaction of cinnamyl-tRNAPhe with Escherichia coli elongation factor Tu.
The products of nitrous acid mediated-deamination of Phe-tRNAPhe from E. coli were analyzed and their capability to interact with elongation factor Tu from E. coli was investigated. Thin-layer chromatography as well as HPLC analysis revealed the existence of at least two deamination products, 3-phenyl-lactyl-tRNAPhe and cinnamyl-tRNAPhe. It could be shown that the aminoacyl-tRNA analogues were active in the formation of the ternary complex with EF-Tu X GTP, although with a lower efficiency than native Phe-tRNAPhe. For both modified acyl-tRNAs the dissociation constant was determined to be 3 X 10(-5) M.
D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000032:analysis*; D006160:Guanosine Triphosphate / Q000378:metabolism; D009608:Nitrous Acid; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*
D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; C037348:tRNA, cinnamylphenylalanine-; C037349:tRNA, phenyllactylphenylalanine-; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu; D009608:Nitrous Acid