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PMID: 6192393 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

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

Nucleic acids research ·Vol. 11 ·No. 14 ·1983-07-25 ·Pages 4823-33

Hu JC, Dahlberg JE

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.

MeSH Terms
Animals Avian Leukosis Virus/enzymology Avian Myeloblastosis Virus/enzymology Base Sequence Chick Embryo Endonucleases Endoribonucleases Nucleic Acid Conformation Pancreas/enzymology Phosphorus Radioisotopes Protein Binding Pseudouridine RNA, Transfer, Amino Acyl/metabolism RNA-Directed DNA Polymerase/metabolism Ribonuclease, Pancreatic Single-Strand Specific DNA and RNA Endonucleases
Chemicals
Phosphorus Radioisotopes RNA, Transfer, Amino Acyl Pseudouridine RNA-Directed DNA Polymerase Endonucleases Endoribonucleases Ribonuclease, Pancreatic Single-Strand Specific DNA and RNA Endonucleases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hu J C
Dahlberg J E
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32 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1983-07-25
Pages
4823-33
Language
English
Region
England
NLM ID
0411011
PMCID
PMC326088
Subset
IM
Grants
NIGMS NIH HHS · 5T32 GMO7215-03 0221 · United States
NCI NIH HHS · CA15166 · United States
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