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Mol. Cells 2013; 36(4): 333-339

Published online October 31, 2013

https://doi.org/10.1007/s10059-013-0119-5

© The Korean Society for Molecular and Cellular Biology

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, and Weontae Lee

Structural Biochemistry and Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-740, Korea, 1Department of Biological Sciences, Institute of Molecular Biology and Genetics, Research Center for Functional Cellulomics, Seoul National University, Seoul 151-742, Korea

Received: April 16, 2013; Revised: July 5, 2013; Accepted: July 8, 2013

Abstract

Mammalian SWI/SNF complexes are evolutionary con-served, ATP-dependent chromatin remodeling units. BAF155 in the SWI/SNF complex contains several highly conser-ved domains, including SANT, SWIRM, and leucine zipper domains. The biological roles of the SWIRM domain re-main 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 chro-matography 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 ?-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 ?M).

Keywords BAF155, NMR spectroscopy, protein-DNA interaction, secondary structure, SWIRM domain

Article

Research Article

Mol. Cells 2013; 36(4): 333-339

Published online October 31, 2013 https://doi.org/10.1007/s10059-013-0119-5

Copyright © The Korean Society for Molecular and Cellular Biology.

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, and Weontae Lee

Structural Biochemistry and Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-740, Korea, 1Department of Biological Sciences, Institute of Molecular Biology and Genetics, Research Center for Functional Cellulomics, Seoul National University, Seoul 151-742, Korea

Received: April 16, 2013; Revised: July 5, 2013; Accepted: July 8, 2013

Abstract

Mammalian SWI/SNF complexes are evolutionary con-served, ATP-dependent chromatin remodeling units. BAF155 in the SWI/SNF complex contains several highly conser-ved domains, including SANT, SWIRM, and leucine zipper domains. The biological roles of the SWIRM domain re-main 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 chro-matography 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 ?-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 ?M).

Keywords: BAF155, NMR spectroscopy, protein-DNA interaction, secondary structure, SWIRM domain

Mol. Cells
Jan 31, 2023 Vol.46 No.1, pp. 1~67
COVER PICTURE
RNAs form diverse shapes and play multiple functions as central molecules of gene expression. In this special issue on RNA, seven minireviews illustrate how basic concepts and recent RNA biology findings are transformed into new and exciting RNA therapeutics.

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