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寡脱氧核糖核苷酸模板的核苷成分及核苷酸间磷酸基团在其与人类DNA聚合酶α结合中的作用

Role of nucleoside components and internucleotide phosphate groups of oligodeoxyribonucleotide template in its binding to human DNA polymerase alpha.

作者信息

Lavrik O I, Levina A S, Nevinsky G A, Podust V N

出版信息

FEBS Lett. 1987 Jun 1;216(2):225-8. doi: 10.1016/0014-5793(87)80694-4.

DOI:10.1016/0014-5793(87)80694-4
PMID:3582674
Abstract

Affinity labelling of human placenta DNA polymerase alpha (EC 2.7.7.7) with the reactive oligodeoxyribonucleotide d(pT)2pCPt2+(NH3)2OH7 was used for quantitative analysis of enzyme interaction with oligodeoxyribonucleotides as templates. Dissociation constants and Gibb's energy values for different oligothymidylates d(pT)nT where n = 1-14 have been evaluated by competitive experiments of these ligands with Pt2+ reagent. The data obtained prove the formation of one Me2+-dependent electrostatic contact and a hydrogen bond between the enzyme and one phosphate of these templates. One may suppose that the hydrophobic interaction of any other monomeric link of oligodeoxyribonucleotides with the enzyme template site takes place.

摘要

使用反应性寡脱氧核糖核苷酸d(pT)2pCPt2+(NH3)2OH7对人胎盘DNA聚合酶α（EC 2.7.7.7）进行亲和标记，用于定量分析该酶与作为模板的寡脱氧核糖核苷酸的相互作用。通过这些配体与Pt2+试剂的竞争性实验，评估了不同寡聚胸苷酸d(pT)nT（其中n = 1 - 14）的解离常数和吉布斯能量值。所获得的数据证明了在酶与这些模板的一个磷酸基团之间形成了一个依赖于Me2+的静电接触和一个氢键。可以推测，寡脱氧核糖核苷酸的任何其他单体连接与酶模板位点之间发生了疏水相互作用。

相似文献

1
Role of nucleoside components and internucleotide phosphate groups of oligodeoxyribonucleotide template in its binding to human DNA polymerase alpha.寡脱氧核糖核苷酸模板的核苷成分及核苷酸间磷酸基团在其与人类DNA聚合酶α结合中的作用
FEBS Lett. 1987 Jun 1;216(2):225-8. doi: 10.1016/0014-5793(87)80694-4.
2
[Eukaryotic and prokaryotic DNA-polymerase. II. The role of internucleotide phosphate groups of a template in its binding with the enzyme].
Bioorg Khim. 1987 Jan;13(1):58-68.
3
[Klenow fragment of DNA-polymerase I from E. coli. III. The role of internucleotide phosphate groups of the matrix in its binding with the enzyme].[来自大肠杆菌的DNA聚合酶I的Klenow片段。III. 模板中核苷酸间磷酸基团在其与酶结合中的作用]
Bioorg Khim. 1989 Jan;15(1):78-89.
4
[DNA-polymerase alpha from human placenta. Effectiveness of interaction between oligothymidylates of different lengths and the template-binding site].
Bioorg Khim. 1986 Mar;12(3):357-68.
5
The mechanism of recognition of templates by DNA polymerases from pro- and eukaryotes as revealed by affinity modification data.
J Biomol Struct Dyn. 1991 Aug;9(1):169-86. doi: 10.1080/07391102.1991.10507901.
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DNA polymerase I (Klenow fragment): role of the structure and length of a template in enzyme recognition.
FEBS Lett. 1989 May 8;248(1-2):97-100. doi: 10.1016/0014-5793(89)80439-9.
7
The efficiency of dNTP complex formation with human placenta DNA polymerase alpha as demonstrated by affinity modification.通过亲和修饰证明的人胎盘DNA聚合酶α形成dNTP复合物的效率。
FEBS Lett. 1987 Jun 1;216(2):221-4. doi: 10.1016/0014-5793(87)80693-2.
8
Protein-nucleic acid interaction in reactions catalyzed with DNA polymerases.DNA聚合酶催化反应中的蛋白质-核酸相互作用。
Biochimie. 1988 May;70(5):655-61. doi: 10.1016/0300-9084(88)90250-7.
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[Effectiveness of complex-formation of nucleotides with human DNA polymerase alpha from data of enzyme modification by reactive nucleotide analogs].[从反应性核苷酸类似物对酶的修饰数据看核苷酸与人类DNA聚合酶α形成复合物的有效性]
Mol Biol (Mosk). 1987 Jul-Aug;21(4):1070-9.
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[Protein-nucleic acid interactions in reactions catalyzed by eukaryotic and prokaryotic DNA-polymerases].[真核生物和原核生物DNA聚合酶催化反应中的蛋白质-核酸相互作用]
Biokhimiia. 1989 May;54(5):757-64.