Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex

Article Abstract:

Nuclear magnetic resonance structure of the Mad-Sin3 complex resulting from PAH2 domain of the mammalian corepressor Sin3A and the transrepression domain SID of human Mad1 exhibits an unusual left-handed four helix for the former and an amphipathic alpha helix for the the latter.

United States, Statistical Data Included, Analysis, Conformational analysis, Structure-activity relationships (Biochemistry), Protein structure

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Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity

Article Abstract:

The Mad protein has been identified as a new member of the basic-helix-loop-helix-Zip protein family. The procedure for identification consisted of screening the lambdagt11 expression library with radiolabeled Max protein. A sequence-specific DNA-binding complex, Mad-Max, was observed for the human Mad protein. The Mad-Max heterodimeric complex may be involved in transcriptional repression.

DNA binding proteins

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Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3

Article Abstract:

A study of the factors that facilitate Mad-Max transcriptional inhibition reveals that the repression occurs through the anchoring of mSin3 to DNA as corepressors and indicates the preservation of the transcriptional repression from yeast to mammals. Two mammalian cDNAs that code for Mad-binding proteins exhibit sequence homology with Sin3 and possess four conserved paired amphipathic helix domains. The Mad-Max E box-binding site is identified by ternary complexes formed by Mad-Max and mSin3. Interactions with mSin3 proteins are abolished and Mad transcriptional repression is inhibited by point mutations in the amphipathic alpha-helical region.

Genetic aspects, Yeast, Yeast (Food product)

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