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 journalArticle

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.

Original languageEnglish
Pages (from-to)2753-2757
Number of pages5
JournalBulletin of the Korean Chemical Society
Volume35
Issue number9
DOIs
Publication statusPublished - 2014 Sep 20

Fingerprint

Fluorescence
Nuclear magnetic resonance
DNA
Integrases
Size exclusion chromatography
DNA sequences
Escherichia coli
Chromatin
Actins
Quenching
Monomers
Proteins
Experiments

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

Lee, Dongju ; Moon, Sunjin ; Yun, Jihye ; Kim, Eunhee ; Cheong, Chaejoon ; Lee, Weontae. / NMR and fluorescence studies of DNA binding domain of INI1/hSNF5. In: Bulletin of the Korean Chemical Society. 2014 ; Vol. 35, No. 9. pp. 2753-2757.
@article{cb8be1bbfed3461c92c4fbbe6a3258dc,
title = "NMR and fluorescence studies of DNA binding domain of INI1/hSNF5",
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.",
author = "Dongju Lee and Sunjin Moon and Jihye Yun and Eunhee Kim and Chaejoon Cheong and Weontae Lee",
year = "2014",
month = "9",
day = "20",
doi = "10.5012/bkcs.2014.35.9.2753",
language = "English",
volume = "35",
pages = "2753--2757",
journal = "Bulletin of the Korean Chemical Society",
issn = "0253-2964",
publisher = "Korean Chemical Society",
number = "9",

}

NMR and fluorescence studies of DNA binding domain of INI1/hSNF5. / Lee, Dongju; Moon, Sunjin; Yun, Jihye; Kim, Eunhee; Cheong, Chaejoon; Lee, Weontae.

In: Bulletin of the Korean Chemical Society, Vol. 35, No. 9, 20.09.2014, p. 2753-2757.

Research output: Contribution to journalArticle

TY - JOUR

T1 - NMR and fluorescence studies of DNA binding domain of INI1/hSNF5

AU - Lee, Dongju

AU - Moon, Sunjin

AU - Yun, Jihye

AU - Kim, Eunhee

AU - Cheong, Chaejoon

AU - Lee, Weontae

PY - 2014/9/20

Y1 - 2014/9/20

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84926675872&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84926675872&partnerID=8YFLogxK

U2 - 10.5012/bkcs.2014.35.9.2753

DO - 10.5012/bkcs.2014.35.9.2753

M3 - Article

AN - SCOPUS:84926675872

VL - 35

SP - 2753

EP - 2757

JO - Bulletin of the Korean Chemical Society

JF - Bulletin of the Korean Chemical Society

SN - 0253-2964

IS - 9

ER -