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Interactions with tRNA Lys induce important structural changes in human immunodeficiency virus reverse transcriptase
Author(s) -
Robert Dominique,
Sallafranque-Andreola Marie-Line,
Bordier Bruno,
Sarih-Cottin Leila,
Tarrago-Litvak Laura,
Graves Pierre Vincent,
Barr Philip J.,
Fournier Michel,
Litvak Simon
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80855-d
Subject(s) - reverse transcriptase , primer binding site , primer (cosmetics) , rna directed dna polymerase , transfer rna , polymerase , retrovirus , biology , dna polymerase , rna , microbiology and biotechnology , dna , virology , virus , chemistry , biochemistry , gene , organic chemistry
Retroviral RNA‐dependent DNA polymerase (reverse transcriptase or RT) uses the 3'OH end of a cellular tRNA as primer to initiate DNA synthesis. Previous work with avian retrovirus has shown that reverse transcriptase is implicated in the selection of cellular virion‐encapsidated tRNAs and has shown that the primer tRNA is positioned on the primer binding site near the 5' end of the viral RNA. These mechanisms support the idea that the retroviral polymerase should form complexes with primer tRNA and the specific encapsidated ones. The genomic sequence of human immunodeficiency virus (HIV) allows the prediction that tRNA Lys 3 is the natural primer. In this article we show, using the mobility shift assay, that recombinant HIV reverse transcriptase is able to form a complex with bovine tRNA Lys . By fluorescence studies and α‐chymotrypsin analysis we have observed a modification of the enzyme conformation when reverse transcriptase is bound to the putative primer tRNA. This structural change is specific for tRNA Lys although the retroviral polymerase is able to interact with other tRNAs.