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Titolo:
A 13-amino acid amphipathic alpha-helix is required for the functional interaction between the transcriptional repressor Mad1 and mSin3A
Autore:
Eilers, AL; Billin, AN; Liu, J; Ayer, DE;
Indirizzi:
Univ Utah, Huntsman Canc Inst, Dept Oncol Sci, Salt Lake City, UT 84112 USA Univ Utah Salt Lake City UT USA 84112 l Sci, Salt Lake City, UT 84112 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 46, volume: 274, anno: 1999,
pagine: 32750 - 32756
SICI:
0021-9258(19991112)274:46<32750:A1AAAI>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-TERMINAL DOMAIN; HISTONE DEACETYLASE; TRANSACTIVATION DOMAIN; N-COR; SECONDARY STRUCTURE; BINDING PROTEIN; COMPLEX; MYC; MAX; SIN3;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Ayer, DE Univ Utah, Huntsman Canc Inst, Dept Oncol Sci, 2000 Circle Hope, Salt LakeCity, UT 84112 USA Univ Utah 2000 Circle Hope Salt Lake City UT USA 84112 84112 USA
Citazione:
A.L. Eilers et al., "A 13-amino acid amphipathic alpha-helix is required for the functional interaction between the transcriptional repressor Mad1 and mSin3A", J BIOL CHEM, 274(46), 1999, pp. 32750-32756

Abstract

Members of the Mad family of bHLHZip proteins heterodimerize with Max and function to repress the transcriptional and transforming activities of the Myc protooncogene. Mad:Max heterodimers repress transcription by recruitinga 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 SinS interaction domain, and the second of four paired amphipathic alpha-helices (PAH2) in mSin3A To better understand the requirements for the interaction between the SID and PAH2, wehave 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 cu-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 mSin3AH/DAC corepressor complex.

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Documento generato il 04/04/20 alle ore 15:08:36