Interaction of dNTP, pyrophosphate and their analogs with the dNTP‐binding sites of E. coli DNA polymerase I Klenow fragment and human DNA polymerase

FEBS Letters

Lavrik, O.I.²  Khomov, V.V.¹  Potapova, I.A.²  Nevinsky, G.A.²  Veniaminova, A.G.² 

[1] Scientific Research Technological Institute of Biologically Active Substances, NPO Vektor, Berdsk, Novosibirsk Region, USSR;Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of the USSR Academy of Sciences, 630090 Novosibirsk, USSR

关键词: Klenow fragment;    Human DNA polymerase α;    Interaction with nucleotides;    FK;    Klenow fragment of E. coli DNA polymerase I;    DPH;    DNA polymerase α from human placenta;   

DOI  :  10.1016/0014-5793(90)80842-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 3',5'-exonuclease center of the Klenow fragment of E. coli DNA polymerase I (FK) was selectively blocked by NaF. The latter was shown to forbid the binding of nucleotides and their analogs to the enzyme exonuclease center. In the presence of poly(dT) · r(pA)₁₀ template · primer complex and NaF, we observed AMP, ADP, ATP, PP_i and dATP to be competitive inhibitors of the FK-catalyzed DNA polymerization. The interactions of the nucleotides with FK and human DNA polymerase α were compared to reveal similarity of binding to the DNA polymerizing centers. Structural components of dNTP and PP_i playing key roles in forming complexes with pro- and eukaryotic DNA polymerases were identified.

【 授权许可】

Unknown