HIV-1 reverse transcriptase specifically interacts with the anticodon domain of its cognate primer tRNA.
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.
Barat
C
C
Labo-Retro Centre de Recherche de Biochimie et Génétique Cellulaires du CNRS, Toulouse, France.
Lullien
V
V
Schatz
O
O
Keith
G
G
Nugeyre
M T
MT
Grüninger-Leitch
F
F
Barré-Sinoussi
F
F
LeGrice
S F
SF
Darlix
J L
JL
D000926:Anticodon / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D002213:Capsid / Q000378:metabolism; D002460:Cell Line; D004586:Electrophoresis; D015497:HIV-1 / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D015151:Immunoblotting; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012343:RNA, Transfer / Q000378:metabolism*; D012345:RNA, Transfer, Amino Acid-Specific / Q000378:metabolism*; D012357:RNA, Transfer, Lys / Q000235:genetics / Q000378:metabolism*; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism*; D014758:Viral Core Proteins / Q000378:metabolism
D000926:Anticodon; D012345:RNA, Transfer, Amino Acid-Specific; D012357:RNA, Transfer, Lys; D014758:Viral Core Proteins; D012343:RNA, Transfer; D012194:RNA-Directed DNA Polymerase