Binding of tryptophanyl-tRNA to the reverse transcriptase of replication-defective avian sarcoma viruses.
The ability of reverse transcriptase to bind to [3H]tryptophanyl-tRNA and to function as DNA polymerase was compared for five temperature-sensitive mutants of avian sarcoma virus. Both activities of the reverse transcriptase were found to be heat labile in LA 335 and LA 336 as compared with the wild-type parents. For the other mutant viruses, LA 338, LA 343, and LA 672, grown at the permissive temperature, the reverse transcriptase was nearly as heat stable as for the wild-type parents in terms of tRNA binding and DNA polymerase. LA 338, LA 343, and LA 672 showed characteristic defects in their reverse transcriptase when propagated at the nonpermissive temperature; namely, tryptophanyl-tRNA binding and DNA polymerase activities were coordinately decreased in these virions. The reduced enzymatic activities were not entirely due to an inactive reverse transcriptase present in the virions, however, but rather lower amounts of enzyme protein incorporated into the virions contributed to the effect, according to assays of reverse transcriptase antigen by radioimmune competition.
D000818:Animals; D001358:Avian Sarcoma Viruses / Q000254:growth & development / Q000378:metabolism*; D002642:Chick Embryo; D046508:Culture Techniques; D003673:Defective Viruses / Q000378:metabolism*; D009154:Mutation; D011485:Protein Binding; D012343:RNA, Transfer / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism*; D013696:Temperature; D014364:Tryptophan / Q000378:metabolism; D014779:Virus Replication
D012367:RNA, Viral; D014364:Tryptophan; D012343:RNA, Transfer; D012194:RNA-Directed DNA Polymerase