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Article

A critical role in structure-specific DNA binding for the acetylatable lysine residues in HMGB1.

The Biochemical journal - 1 May 2008

Assenberg René, Webb Michelle, Connolly Edward, Stott Katherine, Watson Matthew, Hobbs Josie, Thomas Jean O

Abstract excerpt

The structure-specific DNA-binding protein HMGB1 (high-mobility group protein B1) which comprises two tandem HMG boxes (A and B) and an acidic C-terminal tail, is acetylated in vivo at Lys(2) and Lys(11) in the A box. Mutation to alanine of both residues in the isolated A domain, which has a strong preference for pre-bent DNA, abolishes binding to four-way junctions and 88 bp DNA minicircles. The same mutations...

Read the complete abstract on PubMed

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 18241198
DOI: 10.1042/BJ20071613

Genes

HMGB1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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A critical role in structure-specific DNA binding for the acetylatable lysine residues in HMGB1.PMID 18241198Read ↗

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