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Study of interaction of XRCC1 with DNA and proteins of base excision repair by photoaffinity labeling technique

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Abstract

The X-ray repair cross-complementing group 1 (XRCC1) protein plays a central role in base excision repair (BER) interacting with and modulating activity of key BER proteins. To estimate the influence of XRCC1 on interactions of BER proteins poly(ADP-ribose) polymerase 1 (PARP1), apurinic/apyrimidinic endonuclease 1 (APE1), flap endonuclease 1 (FEN1), and DNA polymerase β (Pol β) with DNA intermediates, photoaffinity labeling using different photoreactive DNA was carried out in the presence or absence of XRCC1. XRCC1 competes with APE1, FEN1, and PARP1 for DNA binding, while Pol β increases the efficiency of XRCC1 modification. To study the interactions of XRCC1 with DNA and proteins at the initial stages of BER, DNA duplexes containing a photoreactive group in the template strand opposite the damage were designed. DNA duplexes with 8-oxoguanine or dihydrothymine opposite the photoreactive group were recognized and cleaved by specific DNA glycosylases (OGG1 or NTH1, correspondingly), although the rate of oxidized base excision in the photoreactive structures was lower than in normal substrates. XRCC1 does not display any specificity in recognition of DNA duplexes with damaged bases compared to regular DNA. A photoreactive group opposite a synthetic apurinic/apyrimidinic (AP) site (3-hydroxy-2-hydroxymethyltetrahydrofuran) weakly influences the incision efficiency of AP site analog by APE1. In the absence of magnesium ions, i.e. when incision of AP sites cannot occur, APE1 and XRCC1 compete for DNA binding when present together. However, in the presence of magnesium ions the level of XRCC1 modification increased upon APE1 addition, since APE1 creates nicked DNA duplex, which interacts with XRCC1 more efficiently.

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Abbreviations

APE1:

human apurinic/apyrimidinic endonuclease 1

AP site:

apurinic/apyrimidinic site

BER:

base excision repair

dRP:

deoxyribose phosphate residue

F:

3-hydroxyl-2-hydroxymethyltetrahydrofuran

FEN1:

human flap endonuclease 1

NTH1:

human DNA glycosylase, homolog of E. coli endonuclease III

OGG1:

human 8-oxoguanine DNA glycosylase

8-oxoG:

8-oxoguanine

PARP1:

human poly(ADP-ribose) polymerase 1

Pol β:

rat DNA polymerase β

XRCC1:

human X-ray repair cross-complementing group 1 protein

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Authors and Affiliations

  1. Institute of Chemical Biology and Fundamental Medicine, pr. Akademika Lavrentieva 8, 630090, Novosibirsk, Russia

    Zh. K. Nazarkina, S. N. Khodyreva & O. I. Lavrik

  2. Departement de Radiobiologie et Radiopathologie, UMR 217 CNRS, Commissariat a l’Energie Atomique, BP6, F-92265, Fontenay aux Roses, France

    S. Marsin & J. P. Radicella

Authors
  1. Zh. K. Nazarkina
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  2. S. N. Khodyreva
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  3. S. Marsin
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  4. J. P. Radicella
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  5. O. I. Lavrik
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Correspondence to S. N. Khodyreva.

Additional information

Published in Russian in Biokhimiya, 2007, Vol. 72, No. 8, pp. 1078–1089.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM07-120, July 15, 2007.

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Nazarkina, Z.K., Khodyreva, S.N., Marsin, S. et al. Study of interaction of XRCC1 with DNA and proteins of base excision repair by photoaffinity labeling technique. Biochemistry Moscow 72, 878–886 (2007). https://doi.org/10.1134/S000629790708010X

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  • DOI: https://doi.org/10.1134/S000629790708010X

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