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 language | English (US) |
|---|---|
| Pages (from-to) | 3817-3823 |
| Number of pages | 7 |
| Journal | Journal of Molecular Biology |
| Volume | 427 |
| Issue number | 24 |
| DOIs | |
| State | Published - Dec 4 2015 |
Funding
Funding for this work was provided by an American Heart Association Grant 14GRNT2017003 and the NIH ( 1S10 OD012016 ) to I.R. We thank the Lurie Cancer Center at Northwestern for supporting structural biology research. M.D.C. was supported by Northwestern summer and academic year Undergraduate Research Grants.
Keywords
- NMR spectroscopy
- conformational exchange
- conformational heterogeneity
- multiple binding modes
- protein-protein interaction
ASJC Scopus subject areas
- Molecular Biology
- Structural Biology