Structure and chromosomal DNA binding of the SWIRM domain

Chengmin Qian; Qiang Zhang; Si De Li; Lei Zeng; Martin J. Walsh; Ming Ming Zhou

doi:10.1038/nsmb1022

Structure and chromosomal DNA binding of the SWIRM domain

Chengmin Qian, Qiang Zhang, Si De Li, Lei Zeng, Martin J. Walsh, Ming Ming Zhou

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Abstract

The evolutionarily conserved Swi3p, Rsc8p and Moira (SWIRM) domain is found in many chromosomal proteins involved in chromatin modifications or remodeling. Here we report the three-dimensional solution structure of the SWIRM domain from the human transcriptional adaptor ADA2α. The structure reveals a five-helix bundle consisting of two helix-turn-helix motifs connected by a central long helix, reminiscent of the histone fold. Using structural and biochemical analyses, we showed that the SWIRM domains of human ADA2α and SMARC2 bind to double-stranded and nucleosomal DNA, and we identified amino acid residues required for this function. We demonstrated that the ADA2α SWIRM domain is colocalized with lysine-acetylated histone H3 in the cell nucleus and that it potentiates the ACF remodeling activity by enhancing accessibility of nucleosomal linker DNA bound to histone H1. These data suggest a functional role of the SWIRM domain in chromatin remodeling.

Original language	English
Pages (from-to)	1078-1085
Number of pages	8
Journal	Nature Structural and Molecular Biology
Volume	12
Issue number	12
DOIs	https://doi.org/10.1038/nsmb1022
State	Published - 27 Dec 2005
Externally published	Yes

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title = "Structure and chromosomal DNA binding of the SWIRM domain",

abstract = "The evolutionarily conserved Swi3p, Rsc8p and Moira (SWIRM) domain is found in many chromosomal proteins involved in chromatin modifications or remodeling. Here we report the three-dimensional solution structure of the SWIRM domain from the human transcriptional adaptor ADA2α. The structure reveals a five-helix bundle consisting of two helix-turn-helix motifs connected by a central long helix, reminiscent of the histone fold. Using structural and biochemical analyses, we showed that the SWIRM domains of human ADA2α and SMARC2 bind to double-stranded and nucleosomal DNA, and we identified amino acid residues required for this function. We demonstrated that the ADA2α SWIRM domain is colocalized with lysine-acetylated histone H3 in the cell nucleus and that it potentiates the ACF remodeling activity by enhancing accessibility of nucleosomal linker DNA bound to histone H1. These data suggest a functional role of the SWIRM domain in chromatin remodeling.",

author = "Chengmin Qian and Qiang Zhang and Li, {Si De} and Lei Zeng and Walsh, {Martin J.} and Zhou, {Ming Ming}",

note = "Funding Information: The authors gratefully acknowledge M. Bauck for critical reading of the manuscript, S. Mujtaba for technical help and S. Hearn at Cold Spring Harbor Laboratory Microscopy Facility for technical assistance in performing the confocal laser scanning microscopy. This work was supported by grants from the US National Institutes of Health to M.-M.Z. and M.J.W.",

year = "2005",

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doi = "10.1038/nsmb1022",

language = "English",

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T1 - Structure and chromosomal DNA binding of the SWIRM domain

AU - Qian, Chengmin

AU - Zhang, Qiang

AU - Li, Si De

AU - Zeng, Lei

AU - Walsh, Martin J.

AU - Zhou, Ming Ming

N1 - Funding Information: The authors gratefully acknowledge M. Bauck for critical reading of the manuscript, S. Mujtaba for technical help and S. Hearn at Cold Spring Harbor Laboratory Microscopy Facility for technical assistance in performing the confocal laser scanning microscopy. This work was supported by grants from the US National Institutes of Health to M.-M.Z. and M.J.W.

PY - 2005/12/27

Y1 - 2005/12/27

N2 - The evolutionarily conserved Swi3p, Rsc8p and Moira (SWIRM) domain is found in many chromosomal proteins involved in chromatin modifications or remodeling. Here we report the three-dimensional solution structure of the SWIRM domain from the human transcriptional adaptor ADA2α. The structure reveals a five-helix bundle consisting of two helix-turn-helix motifs connected by a central long helix, reminiscent of the histone fold. Using structural and biochemical analyses, we showed that the SWIRM domains of human ADA2α and SMARC2 bind to double-stranded and nucleosomal DNA, and we identified amino acid residues required for this function. We demonstrated that the ADA2α SWIRM domain is colocalized with lysine-acetylated histone H3 in the cell nucleus and that it potentiates the ACF remodeling activity by enhancing accessibility of nucleosomal linker DNA bound to histone H1. These data suggest a functional role of the SWIRM domain in chromatin remodeling.

AB - The evolutionarily conserved Swi3p, Rsc8p and Moira (SWIRM) domain is found in many chromosomal proteins involved in chromatin modifications or remodeling. Here we report the three-dimensional solution structure of the SWIRM domain from the human transcriptional adaptor ADA2α. The structure reveals a five-helix bundle consisting of two helix-turn-helix motifs connected by a central long helix, reminiscent of the histone fold. Using structural and biochemical analyses, we showed that the SWIRM domains of human ADA2α and SMARC2 bind to double-stranded and nucleosomal DNA, and we identified amino acid residues required for this function. We demonstrated that the ADA2α SWIRM domain is colocalized with lysine-acetylated histone H3 in the cell nucleus and that it potentiates the ACF remodeling activity by enhancing accessibility of nucleosomal linker DNA bound to histone H1. These data suggest a functional role of the SWIRM domain in chromatin remodeling.

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JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

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Structure and chromosomal DNA binding of the SWIRM domain

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