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
Elena S. Dyakonova,
Vladimir V. Koval,
Alexander A. Lomzov,
Alexander A. Ishchenko,
Olga S. Fedorova
Affiliations
Elena S. Dyakonova
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 8 Lavrentyev Ave., Novosibirsk 630090, Russian Federation
Vladimir V. Koval
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
Alexander A. Lomzov
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
Alexander A. Ishchenko
Groupe «Réparation de l׳ADN», Equipe Labellisée par la Ligue Nationale Contre le Cancer, CNRS UMR8200, Univ. Paris-Sud, Université Paris-Saclay, F-94805 Villejuif, France; Gustave Roussy, Université Paris-Saclay, F-94805 Villejuif, France
Olga S. Fedorova
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 8 Lavrentyev Ave., Novosibirsk 630090, Russian Federation; Corresponding author.
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/).
