Structural features required for the binding of tRNATrp to avian myeloblastosis virus reverse transcriptase.
The basis of the specific binding of tRNATrp by avian myeloblastosis virus reverse transcriptase was studied by chemical and enzymatic modification of the RNA. Binding does not depend on recognition of the tryptophan anticodon since molecules cleaved in the anticodon are stably bound by the enzyme. Modification of pseudouridine residues in the tRNA destroys binding to reverse transcriptase. These results are consistent with a model in which reverse transcriptase-tRNATrp interaction occurs not at the anticodon, but at regions in the tRNA which contain or are stabilized by pseudouridine residues.
D000818:Animals; D001354:Avian Leukosis Virus / Q000201:enzymology*; D009189:Avian Myeloblastosis Virus / Q000201:enzymology*; D001483:Base Sequence; D002642:Chick Embryo; D004720:Endonucleases; D004722:Endoribonucleases; D009690:Nucleic Acid Conformation; D010179:Pancreas / Q000201:enzymology; D010761:Phosphorus Radioisotopes; D011485:Protein Binding; D011560:Pseudouridine; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism*; D012259:Ribonuclease, Pancreatic; D015719:Single-Strand Specific DNA and RNA Endonucleases
D010761:Phosphorus Radioisotopes; D012346:RNA, Transfer, Amino Acyl; D011560:Pseudouridine; D012194:RNA-Directed DNA Polymerase; D004720:Endonucleases; D004722:Endoribonucleases; D012259:Ribonuclease, Pancreatic; D015719:Single-Strand Specific DNA and RNA Endonucleases