[NMR paper] Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex.
Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex.
Related ArticlesSolution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex.
J Mol Biol. 2015 Oct 29;
Authors: Clark MD, Zhang Y, Radhakrishnan I
Abstract
The Sds3 transcriptional corepressor facilitates the assembly of the 1-2 megadalton histone deacetylase (HDAC)-associated Sin3L/Rpd3L complex by providing a crucial homo-dimerization 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 7Å 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.
PMID: 26522936 [PubMed - as supplied by publisher]
[NMR paper] Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Angew Chem Int Ed Engl. 2013 Mar 11;52(11):3145-7
Authors: Werbeck ND, Kirkpatrick J,...
NMR profiling of histone deacetylase and acetyl-transferase activities in real time.
NMR profiling of histone deacetylase and acetyl-transferase activities in real time.
NMR profiling of histone deacetylase and acetyl-transferase activities in real time.
ACS Chem Biol. 2011 May 20;6(5):419-24
Authors: Dose A, Liokatis S, Theillet FX, Selenko P, Schwarzer D
Abstract
Histone deacetylases (HDACs) and histone acetyl-transferases (HATs) are universal regulators of eukaryotic transcriptional activity and emerging therapeutic targets for human diseases. Here we describe the generation of isotope-labeled deacetylation and...
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[NMR paper] Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of [
Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of -L-tryptophan.
Related Articles Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of -L-tryptophan.
J Biomol NMR. 1995 Jun;5(4):367-75
Authors: Lee W, Revington M, Farrow NA, Nakamura A, Utsunomiya-Tate N, Miyake Y, Kainosho M, Arrowsmith CH
-L-tryptophan was prepared biosynthetically and its dynamic properties and intermolecular interaction with a complex of Escherichia coli trp-repressor and a 20 base-pair operator DNA were...
Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex.
Linear Mode
