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Interaction of dNTP, pyrophosphate and their analogs with the dNTP‐binding sites of E. coli DNA polymerase I Klenow fragment and human DNA polymerase
Author(s) -
Potapova I.A.,
Nevinsky G.A.,
Veniaminova A.G.,
Khomov V.V.,
Lavrik O.I.
Publication year - 1990
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(90)80842-7
Subject(s) - klenow fragment , dna polymerase i , dna polymerase , dna polymerase ii , dna clamp , primer (cosmetics) , primase , polymerase , exonuclease , microbiology and biotechnology , biochemistry , chemistry , dna , biology , reverse transcriptase , rna , organic chemistry , gene
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.

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