Interaction of primer tRNALys3 with the p51 subunit of human immunodeficiency virus type 1 reverse transcriptase: a possible role in enzyme activation

FEBS Letters

Litvak, Simon¹  Repkova, Marina N.²  Andreola, Marie Line¹  Tarrago-Litvak, Laura¹  Venyaminova, Alija G.²  Nevinsky, Georgyi A.²  Zakharova, Olga D.²  Fournier, Michel¹ 

[1] Institut de Biochimie et Génétique Cellulaires du CNRS, 1 rue Camille Saint Saëns, 33077 Bordeaux cedex, France;Institute of Bioorganic Chemistry, Siberian Division of the Academy of Sciences of Russia, Novosibirsk 630090, Russian Federation

关键词: HIV-1 reverse transcriptase;    tRNALys3 derivative;    Enzyme activation;    RT;    Reverse transcriptase;    HIV-1;    Human immunodeficiency virus type 1;    tRNA(−1);    tRNA derivatives shortened by one;    tRNA(−2);    tRNA derivatives shortened by two;    tRNA(−3);    tRNA derivatives shortened by three nucleotides from the 3′-end;   

DOI  :  10.1016/0014-5793(95)00200-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In the interaction between HIV-1 RT and tRNA^Lys3 each subunit of the heterodimer interacts with tRNA showing a different affinity: K _d (p66) = 23 nM, K _d (p51) = 140 nM. Preincubation of heterodimeric RT with tRNA, at concentrations similar to that of the K _d 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, 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.

【 授权许可】

Unknown