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. 1983 Jul 25;11(14):4823–4833. doi: 10.1093/nar/11.14.4823

Structural features required for the binding of tRNATrp to avian myeloblastosis virus reverse transcriptase.

J C Hu, J E Dahlberg
PMCID: PMC326088  PMID: 6192393

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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