Alanine mutagenesis of high-mobility-group-protein-1 box B (HMG1-B)

Susann Taudte, Hong Xin, Neville R. Kallenbach

Research output: Contribution to journalArticlepeer-review


We have generated a set of alanine-scanning substitutions in high-mobility-group protein 1 box B (HMG1-B; the second domain of the HMG1 nuclear protein from the rat) in order to explore the influence of specific surface side chains on its function and folding. Guanidine hydrochloride and thermal unfolding studies have been carried out to investigate the effect of substituted residues on the folding pathway. Binding to four-way junction and linear-duplex DNA has been assayed to determine which residues play an important role in DNA binding. We have identified several mutants that are more stable or bind more tightly to the junction than the wild-type, including the particular phenylalanine side chain that is thought to intercalate into the DNA. Thus the interaction between HMG1-B and branched DNA substrates should exhibit differences from present models based on the structure of the complexes that have been solved to date.

Original languageEnglish (US)
Pages (from-to)807-814
Number of pages8
JournalBiochemical Journal
Issue number3
StatePublished - May 1 2000


  • Alanine scan
  • Four-way junction
  • Protein stability
  • Protein-DNA interaction
  • Structure-specific recognition

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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