1H, 15N, and 13C resonance assignments and secondary structure of the SWIRM domain of human BAF155, a chromatin remodeling complex component

Sunjin Moon, Joon Shin, Dongju Lee, Rho H. Seong, Weon Tae Lee

Research output: Contribution to journalArticle

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 α-helices that form a typical histone fold for DNA interactions. Our data suggest that the BAF155 SWIRM domain interacts with nucleosome DNA (K d = 0.47 μM).

Original languageEnglish
Pages (from-to)333-339
Number of pages7
JournalMolecules and cells
Volume36
Issue number4
DOIs
Publication statusPublished - 2013 Oct 1

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Chromatin Assembly and Disassembly
DNA
Leucine Zippers
Proteins
Nucleosomes
Affinity Chromatography
Histones
Magnetic Resonance Spectroscopy
Adenosine Triphosphate
Escherichia coli

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

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title = "1H, 15N, and 13C resonance assignments and secondary structure of the SWIRM domain of human BAF155, a chromatin remodeling complex component",
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1H, 15N, and 13C 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 H.; Lee, Weon Tae.

In: Molecules and cells, Vol. 36, No. 4, 01.10.2013, p. 333-339.

Research output: Contribution to journalArticle

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AB - 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 α-helices that form a typical histone fold for DNA interactions. Our data suggest that the BAF155 SWIRM domain interacts with nucleosome DNA (K d = 0.47 μM).

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