The nucleoid-associated protein HU is involved in numerous DNA transactions and thus is essential in DNA maintenance and bacterial survival. The high affinity of HU for SSBs (single-strand breaks) has suggested its involvement in DNA protection, repair and recombination. SSB-containing DNA are major intermediates transiently generated by bifunctional DNA N-glycosylases that initiate the BER (base excision repair) pathway. Enzyme kinetics and DNA-binding experiments demonstrate that HU enhances the 8-oxoguanine-DNA glycosylase activity of Fpg (formamidopyrimidine-DNA glycosylase) by facilitating the release of the enzyme from its final DNA product (one nucleoside gap). We propose that the displacement of Fpg from its end-DNA product by HU is an active mechanism in which HU recognizes the product when it is still bound by Fpg. Through DNA binding, the two proteins interplay to form a transient ternary complex Fpg/DNA/HU which results in the release of Fpg and the molecular entrapment of SSBs by HU. These results support the involvement of HU in BER in vivo.
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Research Article|
September 21 2015
The nucleoid-associated protein HU enhances 8-oxoguanine base excision by the formamidopyrimidine-DNA glycosylase
Rémy Le Meur;
Rémy Le Meur
*Centre de Biophysique Moléculaire (UPR4301), CNRS, rue Charles Sadron, 45 071 Orléans cedex 02, France
†Graduate School of “Santé, Sciences Biologiques et Chimie du Vivant” (ED 549), University of Orléans, Orléans, France
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Françoise Culard;
Françoise Culard
*Centre de Biophysique Moléculaire (UPR4301), CNRS, rue Charles Sadron, 45 071 Orléans cedex 02, France
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Virginie Nadan;
Virginie Nadan
*Centre de Biophysique Moléculaire (UPR4301), CNRS, rue Charles Sadron, 45 071 Orléans cedex 02, France
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Stéphane Goffinont;
Stéphane Goffinont
*Centre de Biophysique Moléculaire (UPR4301), CNRS, rue Charles Sadron, 45 071 Orléans cedex 02, France
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Franck Coste;
Franck Coste
*Centre de Biophysique Moléculaire (UPR4301), CNRS, rue Charles Sadron, 45 071 Orléans cedex 02, France
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Martine Guerin;
Martine Guerin
*Centre de Biophysique Moléculaire (UPR4301), CNRS, rue Charles Sadron, 45 071 Orléans cedex 02, France
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Karine Loth;
Karine Loth
*Centre de Biophysique Moléculaire (UPR4301), CNRS, rue Charles Sadron, 45 071 Orléans cedex 02, France
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Céline Landon;
Céline Landon
*Centre de Biophysique Moléculaire (UPR4301), CNRS, rue Charles Sadron, 45 071 Orléans cedex 02, France
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Bertrand Castaing
Bertrand Castaing
1
*Centre de Biophysique Moléculaire (UPR4301), CNRS, rue Charles Sadron, 45 071 Orléans cedex 02, France
1To whom correspondence should be addressed (email castaing@cnrs-orleans.fr).
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Publisher: Portland Press Ltd
Received:
March 26 2015
Revision Received:
June 19 2015
Accepted:
July 10 2015
Accepted Manuscript online:
July 10 2015
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2015 Authors; published by Portland Press Limited
2015
Biochem J (2015) 471 (1): 13–23.
Article history
Received:
March 26 2015
Revision Received:
June 19 2015
Accepted:
July 10 2015
Accepted Manuscript online:
July 10 2015
Citation
Rémy Le Meur, Françoise Culard, Virginie Nadan, Stéphane Goffinont, Franck Coste, Martine Guerin, Karine Loth, Céline Landon, Bertrand Castaing; The nucleoid-associated protein HU enhances 8-oxoguanine base excision by the formamidopyrimidine-DNA glycosylase. Biochem J 1 October 2015; 471 (1): 13–23. doi: https://doi.org/10.1042/BJ20150387
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