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Summary: A 13-Amino Acid Amphipathic -Helix Is Required for the
Functional Interaction between the Transcriptional Repressor
Mad1 and mSin3A*
(Received for publication, July 30, 1999)
Alanna L. Eilers, Andrew N. Billin, Jun Liu, and Donald E. Ayer§
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 het-
erodimerize with Max and function to repress the tran-
scriptional 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 se-
quences 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 per-
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