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Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2

Author

Listed:
  • Pedro V. Peña

    (Department of Pharmacology)

  • Foteini Davrazou

    (Department of Pharmacology)

  • Xiaobing Shi

    (Stanford University)

  • Kay L. Walter

    (Stanford University)

  • Vladislav V. Verkhusha

    (Albert Einstein College of Medicine)

  • Or Gozani

    (Stanford University)

  • Rui Zhao

    (University of Colorado Health Sciences Center)

  • Tatiana G. Kutateladze

    (Department of Pharmacology)

Abstract

Histones decoded Four papers in this issue tackle the hot topic of chromatin remodelling, specifically, how methyl marks on chromatin are 'read' by the proteins that interact with them. Two report on BPTF (bromodomain and PHD domain transcription factor), a subunit of NURF, the nucleosome remodelling factor. It contains a domain known as a PHD finger, which is shown to bind to histone H3 trimethylated at lysine 4 (H3K4) and to maintain proper activity at developmentally critical HOX genes. The accompanying structural study of the complex explains how the site specificity for H3K4 is achieved. The two other papers reveal that the PHD domain of tumour suppressor ING2 also recognizes trimethylated H3K4, and link the histone mark to repression of transcription. The four papers together establish certain PHD finger domains as previously unrecognized chromatin-binding modules. In a News and Views piece, Peter B. Becker discusses what these papers tell us about the function of the chemical modifications of histone tails.

Suggested Citation

  • Pedro V. Peña & Foteini Davrazou & Xiaobing Shi & Kay L. Walter & Vladislav V. Verkhusha & Or Gozani & Rui Zhao & Tatiana G. Kutateladze, 2006. "Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2," Nature, Nature, vol. 442(7098), pages 100-103, July.
    • Handle: RePEc:nat:nature:v:442:y:2006:i:7098:d:10.1038_nature04814
    DOI: 10.1038/nature04814
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