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Published online before print November 27, 2007, 10.1110/ps.073097308
Protein Science (2008), 17:171-175. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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FOR THE RECORD

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

Yuan He and Ishwar Radhakrishnan

Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500, USA

(RECEIVED June 29, 2007; FINAL REVISION September 19, 2007; ACCEPTED October 4, 2007)

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.

Keywords: Sin3 corepressor; protein–protein interaction; PAH domain; NMR; transcription regulation


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