SRY, like HMG1, recognizes sharp angles in DNA

Simona Ferrari, Vincent R. Harley, Andrea Pontiggia, Peter N. Goodfellow, Robin Lovell-Badge, Marco E. Bianchi

Research output: Contribution to journalArticlepeer-review


HMG boxes are DNA binding domains present in chromatin proteins, general transcription factors for nucleolar and mitochondrial RNA polymerases, and gene- and tissue-specific transcriptional regulators. The HMG boxes of HMG1, an abundant component of chromatin, interact specifically with four-way junctions, DNA structures that are cross-shaped and contain angles of ∼60 and 120° between their arms. We show here also that the HMG box of SRY, the protein that determines the expression of male-specific genes in humans, recognizes four-way junction DNAs irrespective of their sequence. In addition, when SRY binds to linear duplex DNA containing its specific target AACAAAG, it produces a sharp bend. Therefore, the interaction between HMG boxes and DNA appears to be predominantly structure-specific. The production of the recognition of a kink in DNA can serve several distinct functions, such as the repair of DNA lesions, the folding of DNA segments with bound transcriptional factors into productive complexes or the wrapping of DNA in chromatin.

Original languageEnglish
Pages (from-to)4497-4506
Number of pages10
JournalEMBO Journal
Issue number12
Publication statusPublished - 1992


  • Chromatin
  • DNA bending
  • HMG box
  • Protein-DNA interactions
  • Sex determination

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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