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Modulation of YY1 activity by SAP30
Nu En Huang1, Ching Hui Lin, Young Sun Lin
1Graduate Institute of Life Sciences, National Defense Medical Center, ROC, Taipei, Taiwan.
Biochemical and Biophysical Research Communications
|June 6, 2003
Summary
Yin Yang 1 (YY1) transcription factor activity is enhanced by SAP30, a component of the human histone deacetylase complex. This interaction reveals a new mechanism for YY1-mediated gene repression.
Area of Science:
- Molecular Biology
- Gene Regulation
- Epigenetics
Background:
- Yin Yang 1 (YY1) is a conserved, multifunctional transcription factor.
- YY1's activities are modulated by interactions with other proteins.
- SAP30 is a nuclear protein and a component of the human histone deacetylase (HDAC) complex.
Purpose of the Study:
- To investigate the interaction between YY1 and SAP30.
- To elucidate the functional consequence of this interaction on YY1-mediated gene repression.
- To identify the specific domains involved in the YY1-SAP30 interaction.
Main Methods:
- Yeast two-hybrid screening to identify interacting proteins.
- In vitro and in vivo assays to confirm protein-protein interactions.
- Mapping of interaction domains within YY1 and SAP30.
Main Results:
- SAP30 was identified as a protein that associates with YY1.
- SAP30 enhances YY1-mediated repression in a dose-dependent manner.
- Interaction domains were mapped to the C-terminal of YY1 and SAP30.
- YY1, SAP30, and HDAC1 form a complex in vivo, indicating indirect recruitment of HDAC1 by YY1 via SAP30.
Conclusions:
- A novel mechanism for YY1-mediated gene repression involving SAP30 and HDAC1 is described.
- SAP30 acts as a bridge, facilitating YY1's interaction with the HDAC complex.
- This interaction provides new insights into the regulation of gene transcription by YY1.