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


Vol. 35,  No. 9, pp. 2753-2757, Sep.  2014
10.5012/bkcs.2014.35.9.2753


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  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 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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  Cite this article

[IEEE Style]

D. Lee, S. Moon, J. Yun, E. Kim, C. Cheong, W. Lee, "NMR and Fluorescence Studies of DNA Binding Domain of INI1/hSNF5," Bulletin of the Korean Chemical Society, vol. 35, no. 9, pp. 2753-2757, 2014. DOI: 10.5012/bkcs.2014.35.9.2753.

[ACM Style]

Dongju Lee, Sunjin Moon, Jihye Yun, Eunhee Kim, Chaejoon Cheong, and Weontae Lee. 2014. NMR and Fluorescence Studies of DNA Binding Domain of INI1/hSNF5. Bulletin of the Korean Chemical Society, 35, 9, (2014), 2753-2757. DOI: 10.5012/bkcs.2014.35.9.2753.

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ISSN(Print) 0253-2964
ISSN(Online) 1229-5949