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Mlx, a Novel Max-like BHLHZip Protein That Interacts with the Max Network of Transcription Factors*
 

Summary: Mlx, a Novel Max-like BHLHZip Protein That Interacts with the
Max Network of Transcription Factors*
(Received for publication, August 16, 1999)
Andrew N. Billin§¶, Alanna L. Eilers§, Christophe Queva **, and Donald E. Ayer
From the Huntsman Cancer Institute at the University of Utah, Salt Lake City, Utah 84112-5550 and Fred Hutchinson
Cancer Research Center, Division of Basic Sciences, Seattle, Washington, 98109
Mad:Max heterodimers oppose the growth-promoting
action of Myc:Max heterodimers by recruiting the
mSin3-histone deacetylase (mSin3 HDAC) complex to
DNA and functioning as potent transcriptional repres-
sors. There are four known members of the Mad family
that are indistinguishable in their abilities to interact
with Max, bind DNA, repress transcription, and block
Myc Ras co-transformation. To investigate functional
differences between Mad family proteins, we have iden-
tified additional proteins that interact with this family.
Here we present the identification and characterization
of the novel basic-helix-loop-helix zipper protein Mlx
(Max-like protein x), which is structurally and function-
ally related to Max. The similarities between Mlx and

  

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

 

Collections: Biology and Medicine