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MOLECULAR AND CELLULAR BIOLOGY, May 2003, p. 34563467 Vol. 23, No. 10 0270-7306/03/$08.00 0 DOI: 10.1128/MCB.23.10.34563467.2003
 

Summary: MOLECULAR AND CELLULAR BIOLOGY, May 2003, p. 34563467 Vol. 23, No. 10
0270-7306/03/$08.00 0 DOI: 10.1128/MCB.23.10.34563467.2003
Copyright 2003, American Society for Microbiology. All Rights Reserved.
Identification and Characterization of Three New Components
of the mSin3A Corepressor Complex
Tracey C. Fleischer, Ui Jeong Yun, and Donald E. Ayer*
Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah, Salt Lake City, Utah 84112
Received 17 January 2003/Returned for modification 4 February 2003/Accepted 20 February 2003
The mSin3A corepressor complex contains 7 to 10 tightly associated polypeptides and is utilized by many
transcriptional repressors. Much of the corepressor function of mSin3A derives from associations with the
histone deacetylases HDAC1 and HDAC2; however, the contributions of the other mSin3A-associated polypep-
tides remain largely unknown. We have purified an mSin3A complex from K562 erythroleukemia cells and
identified three new mSin3A-associated proteins (SAP): SAP180, SAP130, and SAP45. SAP180 is 40% identical
to a previously identified mSin3A-associated protein, RBP1. SAP45 is identical to mSDS3, the human ortholog
of the SDS3p component of the Saccharomyces cerevisiae Sin3p-Rpd3p corepressor complex. SAP130 does not
have detectable homology to other proteins. Coimmunoprecipitation and gel filtration data suggest that the
new SAPs are, at the very least, components of the same mSin3A complex. Each new SAP repressed tran-
scription when tethered to DNA. Furthermore, repression correlated with mSin3A binding, suggesting that the
new SAPs are components of functional mSin3A corepressor complexes. SAP180 has two repression domains:
a C-terminal domain, which interacts with the mSin3A-HDAC complex, and an N-terminal domain, which

  

Source: Ayer, Don - Huntsman Cancer Institute, University of Utah

 

Collections: Biology and Medicine