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MOLECULAR AND CELLULAR BIOLOGY, 0270-7306/01/$04.00 0 DOI: 10.1128/MCB.21.13.41104118.2001
 

Summary: MOLECULAR AND CELLULAR BIOLOGY,
0270-7306/01/$04.00 0 DOI: 10.1128/MCB.21.13.41104118.2001
July 2001, p. 41104118 Vol. 21, No. 13
Copyright 2001, American Society for Microbiology. All Rights Reserved.
Pf1, a Novel PHD Zinc Finger Protein That Links the TLE
Corepressor to the mSin3A-Histone Deacetylase Complex
GREGORY S. YOCHUM AND DONALD E. AYER*
Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah, Salt Lake City, Utah 84112-5550
Received 26 February 2001/Accepted 10 April 2001
The mSin3A-histone deacetylase corepressor is a multiprotein complex that is recruited by DNA binding
transcriptional repressors. Sin3 has four paired amphipathic alpha helices (PAH1 to -4) that are protein-
protein interaction motifs and is the scaffold upon which the complex assembles. We identified a novel
mSin3A-interacting protein that has two plant homeodomain (PHD) zinc fingers we term Pf1, for PHD factor
one. Pf1 associates with mSin3A in vivo and recruits the mSin3A complex to repress transcription when fused
to the DNA binding domain of Gal4. Pf1 interacts with Sin3 through two independent Sin3 interaction domains
(SIDs), Pf1SID1 and Pf1SID2. Pf1SID1 binds PAH2, while Pf1SID2 binds PAH1. Pf1SID1 has sequence and
structural similarity to the well-characterized 13-amino-acid SID of the Mad bHLHZip repressor. Pf1SID2
does not have sequence similarity with either Mad SID or Pf1SID1 and therefore represents a novel Sin3
binding domain. Mutations in a minimal fragment of Pf1 that encompasses Pf1SID1 inhibited mSin3A binding
yet only slightly impaired repression when targeted to DNA, implying that Pf1 might interact with other

  

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

 

Collections: Biology and Medicine