Solution NMR studies of apo-mSin3A and -mSin3B reveal that the PAH1 and PAH2 domains are structurally independent

Yuan He, Ishwar Radhakrishnan*

*Corresponding author for this work

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

The evolutionarily conserved mammalian Sin3 (mSin3) transcriptional corepressor interacts with a diverse array of transcription factors mainly through two PAH (paired amphipathic helix) domains located near the N terminus. Previous studies suggested the possibility of interdomain interactions involving the PAH domains. Here, we show that the domains are structurally independent and the properties of the individual domains, such as the conformational heterogeneity and the ability of mSin3A PAH2 to homodimerize, are preserved in constructs that span both PAH domains. Our results thus suggest that the N-terminal segments of the Sin3 proteins are broadly available for interactions with other proteins and that the PAH domains are organized into structurally independent modules. Our data also rule out any heterotypic association between the paralogous mSin3A and mSin3B proteins via interactions involving the mSin3A PAH2 domain. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)171-175
Number of pages5
JournalProtein Science
Volume17
Issue number1
DOIs
StatePublished - Jan 2008

Keywords

  • NMR
  • PAH domain
  • Protein-protein interaction
  • Sin3 corepressor
  • Transcription regulation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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