Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding

Ketan S. Gajiwala, Hua Chen, Fabrice Cornille, Bernard P. Roques, Walter Reith, Bernard Mach and Stephen K. Burley ()
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Ketan S. Gajiwala: Laboratories of Molecular Biophysics, Pels Family Center for Biochemistry and Structural Biology
Hua Chen: Laboratories of Molecular Biophysics, Pels Family Center for Biochemistry and Structural Biology
Fabrice Cornille: Départment de Pharmacologie Moléculaire et Structurale, INSERM U266, CNRS URA D1500, UFR des Sciences Pharmaceutiques et Bioligiques
Bernard P. Roques: Départment de Pharmacologie Moléculaire et Structurale, INSERM U266, CNRS URA D1500, UFR des Sciences Pharmaceutiques et Bioligiques
Walter Reith: Départment de Génétique et Microbiologie, Centre Médical Universitaire (CMU)
Bernard Mach: Départment de Génétique et Microbiologie, Centre Médical Universitaire (CMU)
Stephen K. Burley: Laboratories of Molecular Biophysics, Pels Family Center for Biochemistry and Structural Biology

Nature, 2000, vol. 403, issue 6772, 916-921

Abstract: Abstract Regulatory factor X (RFX) proteins are transcriptional activators that recognize X-boxes (DNA of the sequence 5′-GTNRCC(0–3N)RGYAAC-3′, where N is any nucleotide, R is a purine and Y is a pyrimidine) using a highly conserved 76-residue DNA-binding domain (DBD). DNA-binding defects in the protein RFX5 cause bare lymphocyte syndrome or major histocompatibility antigen class II deficiency1. RFX1, -2 and -3 regulate expression of other medically important gene products (for example, interleukin-5 receptor α chain, IL-5Rα)2. Fusions of the ligand-binding domain of the oestrogen receptor with the DBD of RFX4 occur in some human breast tumours3. Here we present a 1.5 Å-resolution structure of two copies of the DBD of human RFX1 (hRFX1) binding cooperatively to a symmetrical X-box4,5. hRFX1 is an unusual member of the winged-helix subfamily of helix–turn–helix proteins6 because it uses a β-hairpin (or wing) to recognize DNA instead of the recognition helix typical of helix–turn–helix proteins. A new model for interactions between linker histones and DNA is proposed.

Date: 2000
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DOI: 10.1038/35002634

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