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HIV‐1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.
Author(s) -
Barat C.,
Lullien V.,
Schatz O.,
Keith G.,
Nugeyre M.T.,
GrüningerLeitch F.,
BarréSinoussi F.,
LeGrice S.F.,
Darlix J.L.
Publication year - 1989
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1989.tb08488.x
Subject(s) - biology , reverse transcriptase , primer binding site , primer (cosmetics) , transfer rna , rna , retrovirus , virology , genetics , rna directed dna polymerase , microbiology and biotechnology , virus , gene , chemistry , organic chemistry
The virion cores of the replication competent type 1 human immunodeficiency virus (HIV‐1), a retrovirus, contain and RNA genome associated with nucleocapsid (NC) and reverse transcriptase (RT p66/p51) molecules. In vitro reconstructions of these complexes with purified components show that NC is required for efficient annealing of the primer tRNALys,3. In the absence of NC, HIV‐1 RT is unable to retrotranscribe the viral RNA template from the tRNA primer. We demonstrate that the HIV‐1 RT p66/p51 specifically binds to its cognate primer tRNALys,3 even in the presence of a 100‐fold molar excess of other tRNAs. Cross‐linking analysis of this interaction locates the contact site to a region within the heavily modified anti‐codon domain of tRNALys,3.