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Interaction of primer tRNA Lys3 with the p51 subunit of human immunodeficiency virus type 1 reverse transcriptase: a possible role in enzyme activation
Author(s) -
Zakharova Olga D.,
Tarrago-Litvak Laura,
Fournier Michel,
Andreola Marie Line,
Repkova Mari.,
Venyaminova Alija G.,
Litvak Simon,
Nevinsky Georgyi A.
Publication year - 1995
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(95)00200-s
Subject(s) - transfer rna , protein subunit , reverse transcriptase , primer (cosmetics) , enzyme , biochemistry , chemistry , nucleotide , rna , biology , microbiology and biotechnology , stereochemistry , gene , organic chemistry
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.