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Structure of IRF-1 with bound DNA reveals determinants of interferon regulation

Author

Listed:
  • Carlos R. Escalante

    (Structural Biology Program, Box 1677, Mount Sinai School of Medicine)

  • Junming Yie

    (Columbia University)

  • Dimitris Thanos

    (Columbia University)

  • Aneel K. Aggarwal

    (Structural Biology Program, Box 1677, Mount Sinai School of Medicine)

Abstract

The family of interferon regulatory factor (IRF) transcription factors is important in the regulation of interferons in response to infection by virus and in the regulation of interferon-inducible genes1,2. The IRF family is characterized by a unique ‘tryptophan cluster’ DNA-binding region. Here we report the crystal structure of the IRF-1 region bound to the natural positive regulatory domain I (PRD I) DNA element from the interferon-β promoter1. The structure provides the first three-dimensional view of a member of the growing IRF family, revealing a new helix–turn–helix motif that latches onto DNA through three of the five conserved tryptophans. The motif selects a short GAAA core sequence through an obliquely angled recognition helix, with an accompanying bending of the DNA axis in the direction of the protein. Together, these features suggest a basis for the occurrence of GAAA repeats within IRF response elements and provide clues to the assembly of the higher-order interferon-β enhancesome.

Suggested Citation

  • Carlos R. Escalante & Junming Yie & Dimitris Thanos & Aneel K. Aggarwal, 1998. "Structure of IRF-1 with bound DNA reveals determinants of interferon regulation," Nature, Nature, vol. 391(6662), pages 103-106, January.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6662:d:10.1038_34224
    DOI: 10.1038/34224
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    Cited by:

    1. Nikolai Schleussner & Pierre Cauchy & Vedran Franke & Maciej Giefing & Oriol Fornes & Naveen Vankadari & Salam A. Assi & Mariantonia Costanza & Marc A. Weniger & Altuna Akalin & Ioannis Anagnostopoulo, 2023. "Transcriptional reprogramming by mutated IRF4 in lymphoma," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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