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Solution structure of SWI1 AT‐rich interaction domain from Saccharomyces cerevisiae and its nonspecific binding to DNA
Author(s) -
Wang Tao,
Zhang Jiahai,
Zhang Xuecheng,
Tu Xiaoming
Publication year - 2012
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24091
Subject(s) - saccharomyces cerevisiae , dna , chromatin , yeast , domain (mathematical analysis) , dna binding domain , chemistry , b3 domain , binding domain , dna binding protein , biochemistry , biophysics , microbiology and biotechnology , binding site , biology , transcription factor , gene , mathematical analysis , mathematics
SWI1 is a subunit of the SWI/SNF complex involved in chromatin remodeling. It contains an AT‐rich interaction domain (ARID) which has the potential DNA binding activity. In this study, we determined the solution structure of the SWI1 ARID domain from Saccharomyces cerevisiae by nuclear magnetic resonance spectroscopy. Yeast SWI1 ARID domain is composed of seven alpha helices, six of which are conserved among the ARID family. In addition, the DNA‐binding activity of the SWI1 ARID domain was confirmed by chemical shift perturbation assay. Similar to its human homolog, the yeast SWI1 ARID domain binds DNA nonspecifically. Proteins 2012; © 2012 Wiley Periodicals, Inc.