Interaction of primer tRNA(Lys3) with the p51 subunit of human immunodeficiency virus type 1 reverse transcriptase: a possible role in enzyme activation.
In the interaction between HIV-1 RT and tRNA(Lys3) each subunit of the heterodimer interacts with tRNA showing a different affinity: Kd (p66) = 23 nM, Kd (p51) = 140 nM. Preincubation of heterodimeric RT with tRNA, at concentrations similar to that of the Kd value for p51, leads to an increase of the catalytic activity on poly(A)-oligo(dT). These results were compared to those using different tRNA analogs: oxidized tRNA, tRNAs lacking one, two or three nucleotides from the 3'-end, or ribo- and deoxyribonucleotides mimicking the anticodon loop sequence. In all cases, tRNA analogs were weaker activators of HIV-1 RT than natural tRNA. A possible mechanism of RT p66/p51 activation by tRNA and its analogs, mediated through the p51 subunit, is discussed.
Zakharova
O D
OD
Institute of Bioorganic Chemistry, Siberian Division of the Academy of Sciences of Russia, Novosibirsk.
Tarrago-Litvak
L
L
Fournier
M
M
Andreola
M L
ML
Repkova
M N
MN
Venyaminova
A G
AG
Litvak
S
S
Nevinsky
G A
GA
D000926:Anticodon; D001483:Base Sequence; D004789:Enzyme Activation; D054303:HIV Reverse Transcriptase; D015497:HIV-1 / Q000201:enzymology; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011485:Protein Binding; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry / Q000378:metabolism*; D012194:RNA-Directed DNA Polymerase / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D013997:Time Factors
D000926:Anticodon; D046911:Macromolecular Substances; D012346:RNA, Transfer, Amino Acyl; D054303:HIV Reverse Transcriptase; D012194:RNA-Directed DNA Polymerase