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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/16239


    Title: The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activities
    Authors: 姚雅莉;Yao, Ya-Li;Yang, WM
    Contributors: 生物科技學系
    Date: 2003-08
    Issue Date: 2012-11-23 17:10:21 (UTC+8)
    Abstract: "The metastasis-associated protein MTA1 has been
    shown to express differentially to high levels in metastatic cells. MTA2, which is homologous to MTA1, is a
    component of the NuRD ATP-dependent chromatin remodeling and histone deacetylase complex. Here we report evidence that although both human MTA1 and
    MTA2 repress transcription specifically, are located in
    the nucleus, and contain associated histone deacetylase
    activity, they exist in two biochemically distinct protein
    complexes and may perform different functions pertaining to tumor metastasis. Specifically, both MTA1 and
    MTA2 complexes exert histone deacetylase activity.
    However, the MTA1 complex contained HDAC1/2,
    RbAp46/48, and MBD3, but not Sin3 or Mi2, two important components of the MTA2 complex. Moreover, the
    MTA2 complex is similar to the HDAC1 complex, suggesting a housekeeping role of the MTA2 complex. The
    MTA1 complex could be further separated, resulting in a
    core MTA1-HDAC complex, showing that the histone
    deacetylase activity and transcriptional repression activity were integral properties of the MTA1 complex.
    Finally, MTA1, unlike MTA2, did not interact with the
    pleotropic transcription factor YY1 or the immunophilin FKBP25. We suggest that MTA1 associates with a
    different set of transcription factors from MTA2 and
    that this property may contribute to the metastatic potential of cells overexpressing MTA1. We also report the
    finding of human MTA3, which is highly homologous to
    both MTA1 and MTA2. However, MTA3 does not repress
    transcription to a significant level and appears to have a
    diffused pattern of subcellular localization, suggesting a
    biological role distinct from that of the other two MTA
    proteins."
    Relation: JOURNAL OF BIOLOGICAL CHEMISTRY
    Appears in Collections:[生物科技學系] 期刊論文

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