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http://dx.doi.org/10.5012/bkcs.2014.35.9.2753

NMR and Fluorescence Studies of DNA Binding Domain of INI1/hSNF5  

Lee, Dongju (Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University)
Moon, Sunjin (Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University)
Yun, Jihye (Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University)
Kim, Eunhee (Magnetic Resonance Team, Korea Basic Science Institute (KBSI))
Cheong, Chaejoon (Magnetic Resonance Team, Korea Basic Science Institute (KBSI))
Lee, Weontae (Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University)
Publication Information
Bulletin of the Korean Chemical Society / v.35, no.9, 2014 , pp. 2753-2757 More about this Journal
Abstract
INtegrase Interactor 1 protein (INI1/hSNF5) or BRG1-associated factor 47 (BAF47) is a SWI/SNF-related matrix associated actin dependent regulator of chromatin subfamily B member. DNA binding domain of INI1/hSNF5 is cloned into E.coli expression vectors, pET32a and purified as a monomer using size exclusion chromatography. NMR data show that $INI1^{DBD}$ has folded state with high population of ${\alpha}$-helices. By fluorescence-quenching experiments, binding affinities between $INI1^{DBD}$ and two double stranded DNA fragments were determined as $29.9{\pm}2.6{\mu}M$ (GAL4_1) and $258.7{\pm}5.8$ (GAL4_2) ${\mu}M$, respectively. Our data revealed that DNA binding domain of INI1/hSNF5 binds to transcriptional DNA sequences, and it could play an important role as a transcriptional regulator.
Keywords
INI1/hSNF5; DNA binding domain; NMR; Purification; Fluorescence;
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