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. 2009 Jul;36(6):1399-404.
doi: 10.1007/s11033-008-9327-z. Epub 2008 Aug 1.

Post-synthetic acetylation of HMGB1 protein modulates its interactions with supercoiled DNA

Iva Ugrinova  1 , Iliya G Pashev, Evdokia A Pasheva
Affiliations

Post-synthetic acetylation of HMGB1 protein modulates its interactions with supercoiled DNA

Iva Ugrinova et al. Mol Biol Rep. 2009 Jul.

Abstract

High mobility group box (HMGB) proteins 1 and 2 are abundant non-histone nuclear proteins that regulate chromatin structure because of their structure-specific binding to DNA. Here, we have investigated how the post-synthetic acetylation of HMGB1 affects its interaction with negatively supercoiled DNA by employing monoacetylated at Lys2 protein, isolated from butyrate-treated cells. Our data reveal that this modification enhances three reaction parameters: binding affinity, supercoiling activity and capacity to protect the supercoiled DNA from relaxation by topoisomerase I. We show that monoacetylation at Lys2 mimics the effect of acidic tail removal but to a lesser extent thus demonstrating that in vivo acetylated HMGB1 is capable of modulating its interaction with negatively supercoiled DNA.

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