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HIV‐1 Reverse transcriptase is capable of elongating derivatives of sequence specific noncomplementary oligodeoxynucleotides
Author(s) -
Martyanov Igor V.,
Zakharova Ol'Ga D.,
Sottofattori Enzo,
Maksakova Galiya A.,
Pyshnyi Dmitry V.,
Mazzei Mauro,
Balbi Alessandro,
Litvak Simon,
TarragoLitvak Laura,
Nevinsky Georgy A.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.7510450502
Subject(s) - reverse transcriptase , chemistry , primer (cosmetics) , human immunodeficiency virus (hiv) , stereochemistry , enzyme , rna , biology , biochemistry , virology , organic chemistry , gene
We have carried out a comparison of K M and V max values for various primers in the polymerization reaction catalyzed by the HIV‐1 RT. The affinity of RT for complementary d(pT) 6 containing two different 5′‐end pyranone derivatives was 2–3 orders of magnitude higher (K M = 3–15 nM) than that of d(pT) 6 (K M = 12.6 mM). Oligodeoxynucleotides (ODNs) noncomplementary to poly(A) template were not elongated by RT. However, derivatives of d(CAGGTG) containing the 5′‐terminal chromone and coumarin related groups were efficient primers showing K M (30–300 nM) and V max (75–93%) values comparable with that for d(pT)10 (800 nM; 100%). The [d(CAGGTG)]ddT ODN derivatives were effective inhibitors of RT. The primer function of derivatives of noncomplementary ODNs appears to be due to the additional interactions of their 5′‐terminal groups with the enzyme tRNA‐binding site.