Structural requirements for binding of bovine tRNATrp with avian myeloblastosis virus DNA polymerase
نویسندگان
چکیده
Avian DNA polymerases use host tRNATrp as the primer for transcription. Bovine tRNATrp has been previously shown to be a biologic substitute for the avian primer. A bovine tRNATrp fragment has been identified as having a high binding affinity for the polymerase. The fragment is assigned to be 67 nucleotides, and contains most of the elements required to maintain the secondary and tertiary structure of tRNATrp.
منابع مشابه
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. The...
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The ability of tryptophan tRNA (tRNATrp) to initiate reverse transcription of the 70S RNA of avian RNA tumor viruses suggested that the reverse transcriptase (RNA-dependent DNA polymerase; deoxynucleosidetriphosphate: DNA deoxynucleotidyltransferase; EC 2.7.7.7) might have a specific binding site for the tRNA. A complex of tRNATrp and the avian myeloblastosis virus reverse transcriptase has bee...
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A complex between tRNATrp (beef) and 35 S RNA from avian myeloblastosis virus is obtained when the mixture is preincubated in the presence of reverse transcriptase at 35 degrees C. The tRNA-RNA complex is active in initiating DNA synthesis catalyzed by reverse transcriptase. The interaction of tRNA with reverse transcriptase involves the partial unwinding of the acceptor stem of tRNA, as eviden...
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The RNA-directed DNA polymerase (deoxynucleosidetriphosphate:DNA deoxynucleotidyltransferase EC 2.7.7.7) of avian oncornavirus requires a tryptophan tRNA (tRNATrp) primer molecule located close to the 5' end of the viral RNA genome for the initiation of DNA synthesis in vitro. In this communication we demonstrate that the DNA product, transcribed from avian myeloblastosis virus (AMV) 35S RNA co...
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Tryptophanyl-tRNA was specifically labeled at the 3' end with [3H]tryptophan and cleaved in half with RNase under denaturing conditions, and the 3' half was shown to hybridize exclusively at the 5' end of avian myeloblastosis virus RNA. The RNA-dependent DNA polymerase of avian myeloblastosis virus is capable of efficiently binding the 3' half of the primer molecule.
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عنوان ژورنال:
- Nucleic acids research
دوره 8 1 شماره
صفحات -
تاریخ انتشار 1980