TY - JOUR

T1 - 5'-Deoxyribose Phosphate Lyase Activity of Apurinic/Apyrimidinic Endonuclease 1

AU - Ilina, E. S.

AU - Lavrik, O. I.

AU - Khodyreva, S. N.

N1 - Funding Information: The work on studying the interaction of proteins with DNA was supported by the Russian Foundation for Basic Research (project no. 17-00-00097), and the stages of production and characteristics of proteins for research were supported by the Russian Science Foundation (grant no. 19-14-00204). Publisher Copyright: © 2021, Pleiades Publishing, Inc. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.

PY - 2021/3

Y1 - 2021/3

N2 - One of the most common DNA lesions is the appearance of apurinic/apyrimidinic (AP-) sites. The main repair pathway for AP sites is initiated by apurinic/apyrimidinic endonuclease 1 (APE1). Upon hydrolysis of the phosphodiester bond by this enzyme, a one nucleotide gap flanked by 3′-hydroxyl and 5′‑deoxyribose phosphate groups on the 5′-side of the AP site is formed. After hydrolysis of the AP site, APE1 remains associated with the product for some time. In the present work, the ability of APE1 to form a product of covalent attachment of APE1 to DNA containing a gap with a 5′-deoxyribose phosphate residue was demonstrated. In addition, it was found that while in a complex with the product of hydrolysis of the AP site, APE1 exhibits 5'‑deoxyribose phosphate lyase activity, cleaving off the 5′-deoxyribose phosphate residue. The presence of lyase activity in APE1 may be important for the repair of AP sites if there is a deficiency of, or mutations in DNA polymerase β, the main enzyme that removes the 5′-deoxyribose phosphate group.

AB - One of the most common DNA lesions is the appearance of apurinic/apyrimidinic (AP-) sites. The main repair pathway for AP sites is initiated by apurinic/apyrimidinic endonuclease 1 (APE1). Upon hydrolysis of the phosphodiester bond by this enzyme, a one nucleotide gap flanked by 3′-hydroxyl and 5′‑deoxyribose phosphate groups on the 5′-side of the AP site is formed. After hydrolysis of the AP site, APE1 remains associated with the product for some time. In the present work, the ability of APE1 to form a product of covalent attachment of APE1 to DNA containing a gap with a 5′-deoxyribose phosphate residue was demonstrated. In addition, it was found that while in a complex with the product of hydrolysis of the AP site, APE1 exhibits 5'‑deoxyribose phosphate lyase activity, cleaving off the 5′-deoxyribose phosphate residue. The presence of lyase activity in APE1 may be important for the repair of AP sites if there is a deficiency of, or mutations in DNA polymerase β, the main enzyme that removes the 5′-deoxyribose phosphate group.

KW - affinity modification

KW - apurinic/apyrimidinic endonuclease 1

KW - apurinic/apyrimidinic sites

KW - deoxyribose phosphate lyase activity

KW - DNA repair

UR - http://www.scopus.com/inward/record.url?scp=85105087921&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/e445786f-5308-3653-aa44-7ebd7cf00c86/

U2 - 10.1134/S0026893321020084

DO - 10.1134/S0026893321020084

M3 - Article

AN - SCOPUS:85105087921

VL - 55

SP - 234

EP - 240

JO - Molecular Biology

JF - Molecular Biology

SN - 0026-8933

IS - 2

ER -