Transient HMGB protein interactions with B-DNA duplexes and complexes

Jeff Zimmerman, L. James Maher

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


HMGB proteins are abundant, non-histone proteins in eukaryotic chromatin. HMGB proteins contain one or two conserved "HMG boxes" and can be sequence-specific or nonspecific in their DNA binding. HMGB proteins cause strong DNA bending and bind preferentially to deformed DNAs. We wish to understand how HMGB proteins increase the apparent flexibility of non-distorted B-form DNA. We test the hypothesis that HMGB proteins bind transiently, creating an ensemble of distorted DNAs with rapidly interconverting conformations. We show that binding of B-form DNA by HMGB proteins is both weak and transient under conditions where DNA cyclization is strongly enhanced. We also detect novel complexes in which HMGB proteins simultaneously bind more than one DNA duplex.

Original languageEnglish (US)
Pages (from-to)79-84
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Jun 20 2008


  • Binding
  • Cruciform
  • DNA
  • Gel shift
  • HMG
  • HMGB
  • Kinetics
  • Kink

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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