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KMID : 0578320130360040333
Molecules and Cells
2013 Volume.36 No. 4 p.333 ~ p.339
1H, 15N, and 13C Resonance Assignments and Secondary Structure of the SWIRM Domain of Human BAF155, a Chromatin Remodeling Complex Component
Moon Sun-Jin

Shin Joon
Lee Dong-Ju
Seong Rho H.
Lee Weon-Tae
Abstract
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 1H, 15N, and 13C resonance assignments and secondary structure of this domain using nuclear magnetic resonance (NMR) spectroscopy and the TALOS+ program. The secondary structure consists of five ¥á-helices that form a typical histone fold for DNA interactions. Our data suggest that the BAF155 SWIRM domain interacts with nucleosome DNA (Kd = 0.47 ¥ìM).
KEYWORD
BAF155, NMR spectroscopy, protein-DNA interaction, secondary structure, SWIRM domain
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