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Properties of 2′,3′‐dideoxy‐2′,3′‐dehydrothymidine 5′‐triphosphate in terminating DNA synthesis catalyzed by several different DNA polymerases
Author(s) -
Dyatkitalia,
Minassian Shahnara,
Kukhanova Marina,
Krayevsky Alexander,
von Janta-Lipinsky Martin,
Chidgeavadze Zurab,
Beabealashvilli Robert
Publication year - 1987
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(87)81208-5
Subject(s) - dna polymerase , dna polymerase ii , primase , dna clamp , polymerase , dna , microbiology and biotechnology , primer (cosmetics) , dna synthesis , dna polymerase i , biology , dna polymerase mu , biochemistry , chemistry , reverse transcriptase , circular bacterial chromosome , polymerase chain reaction , gene , organic chemistry
2′‐3′‐Dideoxy‐2′,3′‐dehydrothymidine 5′‐triphosphate (dddTTP) shows termination substrate properties in the DNA synthesis catalyzed by E. coli DNA polymerase I KF, rat liver DNA polymerase β, reverse transcriptases of avian myeloblastosis virus and Raus sarcoma virus and calf thymus terminal deoxynucleotidyl transferase. This implies that the mononucleotide residue of dddTTP incorporates into 3′‐termini of newly synthesized DNA chains. However, dddTTP has no influence on the DNA synthesis catalyzed by calf thymus DNA polymerase α. In the case of some DNA polymerases dddTTP was one order of magnitude more effective in comparison with the other known termination substrates.