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- Title
NMR and Fluorescence Studies of DNA Binding Domain of INI1/hSNF5.
- Authors
Dongju Lee; Sunjin Moon; Jihye Yun; Eunhee Kim; Chaejoon Cheong; Weontae Lee
- 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.
- Subjects
INTEGRASES; ACTIN research; CHROMATIN; DNA-binding proteins; NUCLEAR magnetic resonance
- Publication
Bulletin of the Korean Chemical Society, 2014, Vol 35, Issue 9, p2753
- ISSN
0253-2964
- Publication type
Article
- DOI
10.5012/bkcs.2014.35.9.2753