Comparison of interactions of 5'-derivatives of deoxyoctathymidylate with human DNA polymerize alpha and HIV reverse transcriptase

S N Khodyreva; V N Podust; D S Sergeev; E M Ivanova; E I Frolova; A A Koshkin; T S Godovikova; V F Zarytova; M Ricchetti; O I Lavrik

doi:10.1007/BF01006894

Comparison of interactions of 5'-derivatives of deoxyoctathymidylate with human DNA polymerize alpha and HIV reverse transcriptase

Mol Biol Rep. 1993 Jun;18(1):43-7. doi: 10.1007/BF01006894.

Authors

S N Khodyreva¹, V N Podust, D S Sergeev, E M Ivanova, E I Frolova, A A Koshkin, T S Godovikova, V F Zarytova, M Ricchetti, O I Lavrik

Affiliation

¹ Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Novosibirsk.

PMID: 7694077
DOI: 10.1007/BF01006894

Abstract

Km and Vmax values for d(pT8) and its derivatives containing various 5'-end groups were estimated in the reaction of DNA polymerization alpha catalyzed by DNA polymerase alpha and HIV-RT. The effect of 5'-end modification of primer is more pronounced in the case of HIV-RT. Strong influence is observed for an intercalating (ethidium) group. The affinity of EtpT8 is 200-fold higher than that of d(pT8). Attachment of Phn-, Dnm- and Hem-groups results in the increase of affinity of modified primer from 10 up to 20 times. For DNA polymerase alpha the influence of modifiers on primer affinity is much weaker. The effect of 5'-end residues on the Vmax values is also more pronounced for HIV RT. The way to improve selective interaction of oligonucleotide derivatives with the primer site of HIV RT is suggested.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

DNA / metabolism
DNA Polymerase II / metabolism*
HIV Reverse Transcriptase
HIV-1 / enzymology*
Humans
Molecular Structure
Poly T / metabolism*
RNA-Directed DNA Polymerase / metabolism*

Substances

Poly T
DNA
HIV Reverse Transcriptase
RNA-Directed DNA Polymerase
DNA Polymerase II