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J Biol Chem, Vol. 274, Issue 46, 32750-32756, November 12, 1999
-Helix Is Required for the
Functional Interaction between the Transcriptional Repressor Mad1
and mSin3A
From the Department of Oncological Sciences, Huntsman Cancer
Institute, University of Utah, Salt Lake City, Utah 84112-5330
Members of the Mad family of bHLHZip proteins
heterodimerize with Max and function to repress the transcriptional and
transforming activities of the Myc proto-oncogene. Mad:Max heterodimers
repress transcription by recruiting a large multi-protein complex
containing the histone deacetylases, HDAC1 and HDAC2, to DNA. The
interaction between Mad proteins and HDAC1/2 is mediated by the
corepressor mSin3A and requires sequences at the amino terminus of the
Mad proteins, termed the SID, for Sin3
interaction domain, and the second of four
paired amphipathic 
-helices
(PAH2) in mSin3A. To better understand the requirements for the
interaction between the SID and PAH2, we have performed mutagenesis and
structural studies on the SID. These studies show that amino acids
8-20 of Mad1 are sufficient for SID:PAH2 interaction. Further, this
minimal 13-residue SID peptide forms an amphipathic -helix in
solution, and residues on the hydrophobic face of the SID helix are
required for interaction with PAH2. Finally, the minimal SID can
function as an autonomous and portable repression domain, demonstrating that it is sufficient to target a functional mSin3A/HDAC corepressor complex.
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