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Cell, Vol. 89, 341347, May 2, 1997, Copyright 1997 by Cell Press Histone Deacetylase Activity Is Required
 

Summary: Cell, Vol. 89, 341347, May 2, 1997, Copyright 1997 by Cell Press
Histone Deacetylase Activity Is Required
for Full Transcriptional Repression by mSin3A
Christian A. Hassig,* Tracey C. Fleischer, Sin3p interacts with the mSin3 interaction domain, or
SID, in the amino terminus of the four Mad family mem-Andrew N. Billin, Stuart L. Schreiber,*
and Donald E. Ayer bers (Ayer et al., 1995; Hurlin et al., 1995; Schreiber-
Agus et al., 1995; Kasten et al., 1996). Mad1, Max, and*Howard Hughes Medical Institute
Department of Chemistry and Chemical Biology mSin3A form ternary complexes capable of binding DNA
(Ayer et al., 1995). Point mutations in the SID domainDepartment of Molecular and Cellular Biology
Harvard University of Mad1 disrupt its ability to bind mSin3A, negate its
function as a transcriptional repressor (Ayer et al., 1995),Cambridge, Massachusetts 02138
Huntsman Cancer Institute and eliminate Mad1 function in several biologicalassays
(Koskinen et al., 1995; Roussel et al., 1996). These find-Department of Oncological Sciences
Division of Molecular Biology and Genetics ings suggest that Mad:Max heterocomplexes repress
transcription by tethering either mSin3A or mSin3B toUniversity of Utah
Salt Lake City, Utah 84112 DNA. A chimeric protein fusing the SID of Mad1 to the
GAL4 DNA-binding domain results in repression of sim-
ple and complex promoters in a manner that is depen-
dent on mSin3 binding, suggesting that targeting mSin3Summary
to DNA is necessary for repression (Ayer et al., 1996).

  

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

 

Collections: Biology and Medicine