Research output: Contribution to journal › Article › peer-review
5'-Deoxyribose Phosphate Lyase Activity of Apurinic/Apyrimidinic Endonuclease 1. / Ilina, E. S.; Lavrik, O. I.; Khodyreva, S. N.
In: Molecular Biology, Vol. 55, No. 2, 03.2021, p. 234-240.Research output: Contribution to journal › Article › peer-review
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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 -
ID: 28503697