Non-canonical interaction of DNA repair proteins with intact and cleaved AP sites

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Non-canonical interaction of DNA repair proteins with intact and cleaved AP sites. / Khodyreva, Svetlana; Lavrik, Olga.

In: DNA Repair, Vol. 90, 102847, 01.06.2020.

Research output: Contribution to journal › Review article › peer-review

Harvard

Khodyreva, S & Lavrik, O 2020, 'Non-canonical interaction of DNA repair proteins with intact and cleaved AP sites', DNA Repair, vol. 90, 102847. https://doi.org/10.1016/j.dnarep.2020.102847

APA

Khodyreva, S., & Lavrik, O. (2020). Non-canonical interaction of DNA repair proteins with intact and cleaved AP sites. DNA Repair, 90, [102847]. https://doi.org/10.1016/j.dnarep.2020.102847

Vancouver

Khodyreva S, Lavrik O. Non-canonical interaction of DNA repair proteins with intact and cleaved AP sites. DNA Repair. 2020 Jun 1;90:102847. Epub 2020 May 5. doi: 10.1016/j.dnarep.2020.102847

Author

Khodyreva, Svetlana ; Lavrik, Olga. / Non-canonical interaction of DNA repair proteins with intact and cleaved AP sites. In: DNA Repair. 2020 ; Vol. 90.

BibTeX

@article{194ee32322804078884c9d6b7db8561a,

title = "Non-canonical interaction of DNA repair proteins with intact and cleaved AP sites",

abstract = "Apurinic/apyrimidinic (AP) sites are widespread lesions in genomic DNA, arising from a number of exogenous and endogenous sources. These DNA lesions are highly mutagenic and demand efficient repair. The review is devoted to data on searching for previously unrecognized proteins capable of interaction with intact or cleaved AP sites. We mainly focused on proteins that form Schiff base upon this interaction. It is important to note that the aldehyde at the deoxyribose C1 atom both in intact and cleaved AP sites can readily react with nucleophiles of proteins. In most cases, these interactions results in processing of AP sites although the process is less efficient as compared to classical AP/dRP lyases. The biological role of these interactions in providing of backup pathways of DNA repair processes is discussed.",

keywords = "ABH1, AP site, Ape1, Base excision repair, Deoxyribose phosphate, DNA-protein cross-link, GAPDH, HMGA, HMGB1, Ku antigen, PARP, XRCC1 INTERACTIONS, RIBOSOMAL-PROTEIN, PHOSPHATE LYASE ACTIVITY, SINGLE-NUCLEOTIDE, BASE EXCISION-REPAIR, POLY(ADP-RIBOSE) POLYMERASE 1, ABASIC SITES, GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE GAPDH, INDUCED CYTOTOXICITY, APURINIC/APYRIMIDINIC SITES",

author = "Svetlana Khodyreva and Olga Lavrik",

year = "2020",

month = jun,

day = "1",

doi = "10.1016/j.dnarep.2020.102847",

language = "English",

volume = "90",

journal = "DNA Repair",

issn = "1568-7864",

publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Non-canonical interaction of DNA repair proteins with intact and cleaved AP sites

AU - Khodyreva, Svetlana

AU - Lavrik, Olga

PY - 2020/6/1

Y1 - 2020/6/1

N2 - Apurinic/apyrimidinic (AP) sites are widespread lesions in genomic DNA, arising from a number of exogenous and endogenous sources. These DNA lesions are highly mutagenic and demand efficient repair. The review is devoted to data on searching for previously unrecognized proteins capable of interaction with intact or cleaved AP sites. We mainly focused on proteins that form Schiff base upon this interaction. It is important to note that the aldehyde at the deoxyribose C1 atom both in intact and cleaved AP sites can readily react with nucleophiles of proteins. In most cases, these interactions results in processing of AP sites although the process is less efficient as compared to classical AP/dRP lyases. The biological role of these interactions in providing of backup pathways of DNA repair processes is discussed.

AB - Apurinic/apyrimidinic (AP) sites are widespread lesions in genomic DNA, arising from a number of exogenous and endogenous sources. These DNA lesions are highly mutagenic and demand efficient repair. The review is devoted to data on searching for previously unrecognized proteins capable of interaction with intact or cleaved AP sites. We mainly focused on proteins that form Schiff base upon this interaction. It is important to note that the aldehyde at the deoxyribose C1 atom both in intact and cleaved AP sites can readily react with nucleophiles of proteins. In most cases, these interactions results in processing of AP sites although the process is less efficient as compared to classical AP/dRP lyases. The biological role of these interactions in providing of backup pathways of DNA repair processes is discussed.

KW - ABH1

KW - AP site

KW - Ape1

KW - Base excision repair

KW - Deoxyribose phosphate

KW - DNA-protein cross-link

KW - GAPDH

KW - HMGA

KW - HMGB1

KW - Ku antigen

KW - PARP

KW - XRCC1 INTERACTIONS

KW - RIBOSOMAL-PROTEIN

KW - PHOSPHATE LYASE ACTIVITY

KW - SINGLE-NUCLEOTIDE

KW - BASE EXCISION-REPAIR

KW - POLY(ADP-RIBOSE) POLYMERASE 1

KW - ABASIC SITES

KW - GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE GAPDH

KW - INDUCED CYTOTOXICITY

KW - APURINIC/APYRIMIDINIC SITES

UR - http://www.scopus.com/inward/record.url?scp=85085557275&partnerID=8YFLogxK

U2 - 10.1016/j.dnarep.2020.102847

DO - 10.1016/j.dnarep.2020.102847

M3 - Review article

C2 - 32492598

AN - SCOPUS:85085557275

VL - 90

JO - DNA Repair

JF - DNA Repair

SN - 1568-7864

M1 - 102847

ER -

ID: 24412283