Structural features required for the binding of tRNATrp to avian myeloblastosis virus reverse transcriptase. | Academic Article individual record
abstract

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.

authors
author list (cited authors)
Hu, J. C., & Dahlberg, J. E.
publication date
1983
published in
keywords
  • RNA-Directed DNA Polymerase
  • Rna, Transfer, Amino Acyl
  • Nucleic Acid Conformation
  • Pancreas
  • Pseudouridine
  • Chick Embryo
  • Protein Binding
  • Avian Myeloblastosis Virus
  • Endoribonucleases
  • Endonucleases
  • Base Sequence
  • Avian Leukosis Virus
  • Ribonuclease, Pancreatic
  • Phosphorus Radioisotopes
  • Animals
  • Single-Strand Specific DNA And RNA Endonucleases
citation count

16