Premium
3′‐Hydroxymethyl 2′‐deoxynucleoside 5′‐triphosphates are inhibitors highly specific for reverse transcriptase
Author(s) -
Kutateladze Tamara V.,
Kritzyn Anatoli M.,
Florentjev Vladimir L.,
Kavsan Vadim M.,
Chidgeavadze Zurab G.,
Beabealashvilli Robert Sh.
Publication year - 1986
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(86)81489-2
Subject(s) - dna polymerase , klenow fragment , dna polymerase i , polymerase , dna polymerase ii , dna clamp , microbiology and biotechnology , terminator (solar) , reverse transcriptase , primer (cosmetics) , biology , primase , dna polymerase mu , dna , biochemistry , chemistry , polymerase chain reaction , circular bacterial chromosome , exonuclease , gene , ionosphere , physics , astronomy , organic chemistry
dNTP(3′‐OCH 3 ), a 3′‐ O ‐methyl derivative of dNTP, is a chain terminator substrate for DNA synthesis catalyzed by AMV reverse transriptase. The enzyme seems to be the only DNA polymerase susceptible to the inhibitor while all the other DNA polymerases tested are fully resistant to the nucleotide analog. The resistant polymerases are: E. coli DNA polymerase I, Klenow's fragment of DNA polymerase I, phage T 4 DNA polymerase, calf thymus DNA polymerase α, rat liver DNA polymerase β and calf thymus terminal deoxyribonucleotidyl transferase.