H, N, and C resonance assignments and secondary structure of the SWIRM domain of human BAF155, a chromatin remodeling complex component

Moon, Sunjin; Shin, Joon; Lee, Dongju; Seong, Rho; Lee, Weontae
October 2013
Molecules & Cells (Springer Science & Business Media B.V.);Oct2013, Vol. 36 Issue 4, p333
Academic Journal
Mammalian SWI/SNF complexes are evolutionary conserved, ATP-dependent chromatin remodeling units. BAF155 in the SWI/SNF complex contains several highly conserved domains, including SANT, SWIRM, and leucine zipper domains. The biological roles of the SWIRM domain remain unclear; however, both structural and biochemical analyses of this domain have suggested that it could mediate protein-protein or protein-DNA interactions during the chromatin remodeling process. The human BAF155 SWIRM domain was cloned into the Escherichia coli expression vector pMAL-c2X and purified using affinity chromatography for structural analysis. We report the backbone H, N, and C resonance assignments and secondary structure of this domain using nuclear magnetic resonance (NMR) spectroscopy and the TALOS+ program. The secondary structure consists of five α-helices that form a typical histone fold for DNA interactions. Our data suggest that the BAF155 SWIRM domain interacts with nucleosome DNA ( K = 0.47 μM).


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