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来自[具体来源]的核酸内切酶Apn1与含有5,6-二氢尿嘧啶和2-氨基嘌呤的DNA底物相互作用的聚丙烯酰胺凝胶电泳（PAGE）分析和分子动力学（MD）模拟数据。

Data on PAGE analysis and MD simulation for the interaction of endonuclease Apn1 from with DNA substrates containing 5,6-dihydrouracyl and 2-aminopurine.

作者信息

Dyakonova Elena S, Koval Vladimir V, Lomzov Alexander A, Ishchenko Alexander A, Fedorova Olga S

机构信息

Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 8 Lavrentyev Ave., Novosibirsk 630090, Russian Federation.

Department of Natural Sciences, Novosibirsk State University, 2 Pirogov St., Novosibirsk 630090, Russian Federation.

出版信息

Data Brief. 2018 Sep 12;20:1515-1524. doi: 10.1016/j.dib.2018.09.007. eCollection 2018 Oct.

DOI:10.1016/j.dib.2018.09.007
PMID:30671502
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6334592/
Abstract

This article presents new data on nucleotide incision repair (NIR) activity of apurinic/apyrimidinic endonuclease Apn1 of , which is known as a key player of the base excision DNA repair (BER) pathway, see "Yeast structural gene (APN1) for the major apurinic endonuclease: homology to Escherichia coli endonuclease IV" [1], "Abasic sites in DNA: repair and biological consequences in Saccharomyces cerevisiae" [2] and "Characterisation of new substrate specificities of Escherichia coli and Saccharomyces cerevisiae AP endonucleases" [3]. The characterization of NIR activity of wild type Apn1 and mutant form Ape1 H83A were made by denaturing PAGE analysis, and MD simulations of Apn1 complexed with DNA containing 5,6-dihydro-2'-deoxyuridine (DHU) and 2-aminopurine (2-aPu) residues. This data article is associated to the manuscript titled "Apurinic/apyrimidinic endonuclease Apn1 from is recruited to the nucleotide incision repair pathway: kinetic and structural features" [4]. http://creativecommons.org/licenses/by/4.0/

摘要

本文展示了关于嗜热栖热放线菌脱嘌呤/脱嘧啶内切核酸酶Apn1的核苷酸切口修复（NIR）活性的新数据，Apn1是碱基切除DNA修复（BER）途径的关键参与者，见“酵母主要脱嘌呤内切核酸酶的结构基因（APN1）：与大肠杆菌内切核酸酶IV的同源性”[1]、“DNA中的无碱基位点：酿酒酵母中的修复及生物学后果”[2]以及“大肠杆菌和酿酒酵母AP内切核酸酶新底物特异性的表征”[3]。通过变性聚丙烯酰胺凝胶电泳分析以及对与含有5,6 - 二氢 - 2'-脱氧尿苷（DHU）和2 - 氨基嘌呤（2 - aPu）残基的DNA复合的Apn1进行分子动力学模拟，对野生型Apn1和突变形式Ape1 H83A的NIR活性进行了表征。本数据文章与题为“嗜热栖热放线菌的脱嘌呤/脱嘧啶内切核酸酶Apn1被招募到核苷酸切口修复途径：动力学和结构特征”[4]的手稿相关。http://creativecommons.org/licenses/by/4.0/

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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cde4/6334592/f8d67973ecce/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cde4/6334592/d38455543685/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cde4/6334592/fd4a0e91f327/gr8.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cde4/6334592/7dcfec62058b/gr11.jpg

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本文引用的文献

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2
The role of His-83 of yeast apurinic/apyrimidinic endonuclease Apn1 in catalytic incision of abasic sites in DNA.酵母脱嘌呤/脱嘧啶内切酶Apn1的组氨酸83在DNA中无碱基位点催化切割中的作用。
Biochim Biophys Acta. 2015 Jun;1850(6):1297-309. doi: 10.1016/j.bbagen.2015.03.001. Epub 2015 Mar 10.
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Validation of metal-binding sites in macromolecular structures with the CheckMyMetal web server.
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