Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation

DOI Web Site 被引用文献14件
  • Andrei Kuzmichev
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
  • Raphael Margueron
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
  • Alejandro Vaquero
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
  • Tanja S. Preissner
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
  • Michael Scher
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
  • Antonis Kirmizis
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
  • Xuesong Ouyang
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
  • Neil Brockdorff
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
  • Cory Abate-Shen
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
  • Peggy Farnham
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
  • Danny Reinberg
    Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...

抄録

<jats:p> Changes in the substrate specificities of factors that irreversibly modify the histone components of chromatin are expected to have a profound effect on gene expression through epigenetics. Ezh2 is a histone-lysine methyltransferase with activity dependent on its association with other components of the Polycomb Repressive Complexes 2 and 3 (PRC2/3). Ezh2 levels are increasingly elevated during prostate cancer progression. Other PRC2/3 components also are elevated in cancer cells. Overexpression of Ezh2 in tissue culture promotes formation of a previously undescribed PRC complex, PRC4, that contains the NAD <jats:sup>+</jats:sup> -dependent histone deacetylase SirT1 and isoform 2 of the PRC component Eed. Eed2 is expressed in cancer and undifferentiated embryonic stem (ES) cells but is undetectable in normal and differentiated ES cells. The distinct PRCs exhibit differential histone substrate specificities. These findings suggest that formation of a transformation-specific PRC complex may have a major role in resetting patterns of gene expression by regulating chromatin structure. </jats:p>

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