NMR and fluorescence studies of DNA binding domain of INI1/hSNF5

Dongju Lee, Sunjin Moon, Jihye Yun, Eunhee Kim, Chaejoon Cheong, Weontae Lee

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)2753-2757
Number of pages5
JournalBulletin of the Korean Chemical Society
Issue number9
Publication statusPublished - 2014 Sept 20

Bibliographical note

Publisher Copyright:
© 2014, Korean Chemical Society. All rights reserved.

All Science Journal Classification (ASJC) codes

  • Chemistry(all)


Dive into the research topics of 'NMR and fluorescence studies of DNA binding domain of INI1/hSNF5'. Together they form a unique fingerprint.

Cite this