Poly(U)-dependent polyphenylalanine and polytyrosine synthesis in vitro by a tRNATyr variant with an enzymatically altered anticodon, G-A-A.
A variant of T. utilis tRNATyr containing a base substitution (psi----A) in the middle position of the anticodon has been constructed by enzymatic procedures in vitro. This variant is unique in that it can accept both tyrosine and phenylalanine. This tRNA was shown to be active in transferring both tyrosine and phenylalanine into polypeptides in a cell-free, poly (U)-directed translation system from yeast. This result gives further support to the adapter hypothesis since tyrosine, attached to the variant tRNATyr with an anticodon G-A-A, is incorporated into polypeptides in response to poly (U) message.
D000926:Anticodon / Q000235:genetics*; D001483:Base Sequence; D002175:Candida / Q000235:genetics; D014644:Genetic Variation; D007700:Kinetics; D009690:Nucleic Acid Conformation; D010455:Peptides / Q000138:chemical synthesis*; D011072:Poly U; D012343:RNA, Transfer / Q000235:genetics*; D012346:RNA, Transfer, Amino Acyl / Q000235:genetics*
D000926:Anticodon; D010455:Peptides; D012346:RNA, Transfer, Amino Acyl; D011072:Poly U; C012001:polyphenylalanine; C017663:polytyrosine; D012343:RNA, Transfer