HMGB1 interacts differentially with members of the Rel family of transcription factors

Alessandra Agresti, Rossella Lupo, Marco E. Bianchi, Susanne Müller

Research output: Contribution to journalArticle

Abstract

HMGB1 is an architectural factor that enhances the DNA binding affinity of several proteins. We have investigated the influence of HMGB1 on DNA binding by members of the Rel family. HMGB1 enhances DNA binding by p65/p50 and p50/p50, but reduces binding by p65/p65, c-Rel/c-Rel, p65/c-Rel, and p50/c-Rel. In pull-down assays, HMGB1 interacts directly with the p50 subunit via its HMG boxes and this interaction is weakened by the presence of the acidic tail. Functionally, HMGB1 is required for the NF-κB-dependent expression of the adhesion molecule VCAM-1.

Original languageEnglish
Pages (from-to)421-426
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume302
Issue number2
DOIs
Publication statusPublished - Jan 10 2003

Keywords

  • HMGB1
  • NF-κB
  • Protein-protein interaction
  • Rel proteins
  • Transcription

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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