The nucleoid-associated protein HU enhances 8-oxoguanine base excision by the formamidopyrimidine-DNA glycosylase.

Le Meur R, Culard F, Nadan V, Goffinont S, Coste F, Guerin M, Loth K, Landon C, Castaing B
Biochem J. 2015 471 (1): 13-23

PMID: 26392572 · DOI:10.1042/BJ20150387

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.

© 2015 Authors; published by Portland Press Limited.

MeSH Terms (8)

DNA, Bacterial DNA-Binding Proteins DNA-Formamidopyrimidine Glycosylase DNA Breaks, Double-Stranded DNA Repair Escherichia coli Escherichia coli Proteins Guanine

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