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The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain

Author

Listed:
  • Chao Xu

    (Structural Genomics Consortium, University of Toronto)

  • Chuanbing Bian

    (Structural Genomics Consortium, University of Toronto)

  • Robert Lam

    (Structural Genomics Consortium, University of Toronto)

  • Aiping Dong

    (Structural Genomics Consortium, University of Toronto)

  • Jinrong Min

    (Structural Genomics Consortium, University of Toronto
    University of Toronto)

Abstract

CFP1 is a CXXC domain-containing protein and an essential component of the SETD1 histone H3K4 methyltransferase complex. CXXC domain proteins direct different chromatin-modifying activities to various chromatin regions. Here, we report crystal structures of the CFP1 CXXC domain in complex with six different CpG DNA sequences. The crescent-shaped CFP1 CXXC domain is wedged into the major groove of the CpG DNA, distorting the B-form DNA, and interacts extensively with the major groove of the DNA. The structures elucidate the molecular mechanism of the non-methylated CpG-binding specificity of the CFP1 CXXC domain. The CpG motif is confined by a tripeptide located in a rigid loop, which only allows the accommodation of the non-methylated CpG dinucleotide. Furthermore, we demonstrate that CFP1 has a preference for a guanosine nucleotide following the CpG motif.

Suggested Citation

  • Chao Xu & Chuanbing Bian & Robert Lam & Aiping Dong & Jinrong Min, 2011. "The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain," Nature Communications, Nature, vol. 2(1), pages 1-8, September.
    • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1237
    DOI: 10.1038/ncomms1237
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    1. Seung Chel Yang & Mira Park & Kwon-Ho Hong & Hyeonwoo La & Chanhyeok Park & Peike Wang & Gaizhen Li & Qionghua Chen & Youngsok Choi & Francesco J. DeMayo & John P. Lydon & David G. Skalnik & Hyunjung , 2023. "CFP1 governs uterine epigenetic landscapes to intervene in progesterone responses for uterine physiology and suppression of endometriosis," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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