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- W2026779058 abstract "We utilized NTP analogues containing modified bases to probe the mechanism of NTP selection by the primase activity of the herpes simplex virus 1 helicase−primase complex. Primase readily bound NTP analogues of varying base shape, hydrophobicity, and hydrogen-bonding capacity. Remarkably, primase strongly discriminated against incorporating virtually all of the analogues, even though this enzyme misincorporates natural NTPs at frequencies as high as 1 in 7. This included analogues with bases much more hydrophobic than a natural base (e.g., 4- and 7-trifluoromethylbenzimidazole), a base of similar hydrophobicity as a natural base but with the Watson−Crick hydrogen-bonding groups in unusual positions (7-β-d-guanine), bases shaped almost identically to the natural bases (4-aminobenzimidazole and 4,6-difluorobenzimidazole), bases shaped very differently than a natural base (e.g., 5- and 6-trifluoromethylbenzimidazole), and bases capable of forming just one Watson−Crick hydrogen bond with the template base (purine and 4-aminobenzimidazole). The only analogues that primase readily polymerized into primers (ITP and 3-deaza-ATP) were those capable of forming Watson−Crick hydrogen bonds with the template base. Thus, herpes primase appears to require the formation of Watson−Crick hydrogen bonds in order to efficiently polymerize a NTP. In contrast to primase's narrow specificity for NTP analogues, the DNA-dependent NTPase activity associated with the herpes primase−helicase complex exhibited very little specificity with respect to NTPs containing unnatural bases. The implications of these results with respect to the mechanism of the helicase−primase and current fidelity models are discussed." @default.
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- W2026779058 date "2005-11-01" @default.
- W2026779058 modified "2023-10-17" @default.
- W2026779058 title "Herpes Simplex Virus 1 Primase Employs Watson−Crick Hydrogen Bonding To Identify Cognate Nucleoside Triphosphates" @default.
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- W2026779058 doi "https://doi.org/10.1021/bi0513711" @default.
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