Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex

Michael David Clark, Yongbo Zhang, Ishwar Radhakrishnan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

The Sds3 transcriptional corepressor facilitates the assembly of the 1- to 2-MDa histone deacetylase-associated Sin3L/Rpd3L complex by providing a crucial homodimerization activity. Sds3 engages the scaffolding protein Sin3A, via a bipartite motif within the Sin3 interaction domain (SID) comprising a helix and an extended segment. Here, we show that the SID samples two discrete, substantially populated conformations with lifetimes in the tens of milliseconds range. The two conformations differ via a translation of the main chain and the corresponding side chains in the 5- to 7-Å range. Given the close proximity of the SID to other functional motifs in Sds3 at the sequence level, the conformational exchange has the potential to regulate these activities.

Original languageEnglish (US)
Pages (from-to)3817-3823
Number of pages7
JournalJournal of Molecular Biology
Volume427
Issue number24
DOIs
StatePublished - Dec 4 2015

Keywords

  • NMR spectroscopy
  • conformational exchange
  • conformational heterogeneity
  • multiple binding modes
  • protein-protein interaction

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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