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

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Data on PAGE analysis and MD simulation for the interaction of endonuclease Apn1 from Saccharomyces cerevisiae with DNA substrates containing 5,6-dihydrouracyl and 2-aminopurine. / Dyakonova, Elena S.; Koval, Vladimir V.; Lomzov, Alexander A. et al.

In: Data in Brief, Vol. 20, 01.10.2018, p. 1515-1524.

Research output: Contribution to journal › Article › peer-review

BibTeX

@article{6389d0146180493bac3a77709fa2a5be,

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

abstract = "This article presents new data on nucleotide incision repair (NIR) activity of apurinic/apyrimidinic endonuclease Apn1 of Saccharomyces cerevisiae, 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 Saccharomyces cerevisiae is recruited to the nucleotide incision repair pathway: kinetic and structural features” [4]. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).",

keywords = "ESCHERICHIA-COLI, ABASIC SITES, AMBER, BINDING, REPAIR, COORDINATION, INCISION, PROTEINS",

author = "Dyakonova, {Elena S.} and Koval, {Vladimir V.} and Lomzov, {Alexander A.} and Ishchenko, {Alexander A.} and Fedorova, {Olga S.}",

note = "Publisher Copyright: {\textcopyright} 2018 The Authors",

year = "2018",

month = oct,

day = "1",

doi = "10.1016/j.dib.2018.09.007",

language = "English",

volume = "20",

pages = "1515--1524",

journal = "Data in Brief",

issn = "2352-3409",

publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Data on PAGE analysis and MD simulation for the interaction of endonuclease Apn1 from Saccharomyces cerevisiae with DNA substrates containing 5,6-dihydrouracyl and 2-aminopurine

AU - Dyakonova, Elena S.

AU - Koval, Vladimir V.

AU - Lomzov, Alexander A.

AU - Ishchenko, Alexander A.

AU - Fedorova, Olga S.

PY - 2018/10/1

Y1 - 2018/10/1

N2 - This article presents new data on nucleotide incision repair (NIR) activity of apurinic/apyrimidinic endonuclease Apn1 of Saccharomyces cerevisiae, 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 Saccharomyces cerevisiae is recruited to the nucleotide incision repair pathway: kinetic and structural features” [4]. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

AB - This article presents new data on nucleotide incision repair (NIR) activity of apurinic/apyrimidinic endonuclease Apn1 of Saccharomyces cerevisiae, 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 Saccharomyces cerevisiae is recruited to the nucleotide incision repair pathway: kinetic and structural features” [4]. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

KW - ESCHERICHIA-COLI

KW - ABASIC SITES

KW - AMBER

KW - BINDING

KW - REPAIR

KW - COORDINATION

KW - INCISION

KW - PROTEINS

UR - http://www.scopus.com/inward/record.url?scp=85053806205&partnerID=8YFLogxK

U2 - 10.1016/j.dib.2018.09.007

DO - 10.1016/j.dib.2018.09.007

M3 - Article

C2 - 30671502

AN - SCOPUS:85053806205

VL - 20

SP - 1515

EP - 1524

JO - Data in Brief

JF - Data in Brief

SN - 2352-3409

ER -

ID: 16703180