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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 35, Number 9
BKCSDE 35(9)
September 20, 2014 

NMR and Fluorescence Studies of DNA Binding Domain of INI1/hSNF5
Dongju Lee, Sunjin Moon, Jihye Yun, Eunhee Kim, Chaejoon Cheong, Weontae Lee*
INI1/hSNF5, DNA binding domain, NMR, Purification, Fluorescence
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 INI1DBD has folded state with high population of α-helices. By fluorescence-quenching experiments, binding affinities between INI1DBD and two double stranded DNA fragments were determined as 29.9 ± 2.6 μM (GAL4_1) and 258.7 ± 5.8 (GAL4_2) μM, 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.
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