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PMID: 18670905 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Molecular biology reports ·Vol. 36 ·No. 6 ·2009-07-00 ·Pages 1399-404

Ugrinova I, Pashev IG, Pasheva EA

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.

MeSH Terms
Acetylation Butyrates DNA Topoisomerases, Type I/metabolism DNA, Superhelical/metabolism HMGB1 Protein/metabolism Humans Lysine/metabolism Protein Binding Protein Processing, Post-Translational Tumor Cells, Cultured
Chemicals
Butyrates DNA, Superhelical HMGB1 Protein DNA Topoisomerases, Type I Lysine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ugrinova Iva
Institute of Molecular biology, Bulgarian Academy of Sciences, 1113, Sofia, Bulgaria.
Pashev Iliya G
Pasheva Evdokia A
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Article Info
Journal
Molecular biology reports
Abbr.
Mol Biol Rep
ISSN
1573-4978
DOI
10.1007/s11033-008-9327-z
Published
2009-07-00
Epub
2008-00-01
Pages
1399-404
Language
English
Region
Netherlands
NLM ID
0403234
Subset
IM
External Links
PubMed source DOI: 10.1007/s11033-008-9327-z View journal details
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