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Nucleic Acids Research, 1983, Vol. 11, No. 14 4823-4833
© 1983

MOLECULAR BIOLOGY

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

James C. Hu+ and James E. Dahlberg

Department of Physiological Chemistry, University of Wisconsin-Madison Madison, WI 53706, USA

Received April 11, 1983. Accepted June 27, 1983.

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 pseudourldine 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.

+Present address: Department of Bacteriology, University of Wisconsin, Madison, WI 53706, USA


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