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- Title
Structure and chromosomal DNA binding of the SWIRM domain.
- Authors
Chengmin Qian; Qiang Zhang; SiDe Li; Lei Zeng; Walsh, Martin J.; Ming-Ming Zhou
- 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.
- Publication
Nature Structural & Molecular Biology, 2005, Vol 12, Issue 12, p1078
- ISSN
1545-9993
- Publication type
Academic Journal
- DOI
10.1038/nsmb1022