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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 09:10:21 (UTC+0) |
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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