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Extension of the binding motif of the Sin3 interacting domain of the Mad family proteins.

Abstract：

:Sin3 forms the scaffold for a multiprotein corepressor complex that silences transcription via the action of histone deacetylases. Sin3 is recruited to the DNA by several DNA binding repressors, such as the helix-loop-helix proteins of the Mad family. Here, we elaborate on the Mad-Sin3 interaction based on a binding study, solution structure, and dynamics of the PAH2 domain of mSin3 in complex to an extended Sin3 interacting domain (SID) of 24 residues of Mad1. We show that SID residues Met7 and Glu23, outside the previously defined minimal binding motif, mediate additional hydrophobic and electrostatic interactions with PAH2. On the basis of these results we propose an extended consensus sequence describing the PAH2-SID interaction specifically for the Mad family, showing that residues outside the hydrophobic core of the SID interact with PAH2 and modulate binding affinity to appropriate levels.

journal_name

Biochemistry

journal_title

Biochemistry

authors

van Ingen H,Lasonder E,Jansen JF,Kaan AM,Spronk CA,Stunnenberg HG,Vuister GW

doi

10.1021/bi0355645

subject

Has Abstract

pub_date

2004-01-13 00:00:00

pages

46-54

issue

1

eissn

0006-2960

issn

1520-4995

journal_volume

43

pub_type

杂志文章

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