The architecture of ArgR-DNA complexes at the genome-scale in Escherichia coliopen access
- Authors
- Cho, Suhyung; Cho, Yoo-Bok; Kang, Taek Jin; Kim, Sun Chang; Palsson, Bernhard; Cho, Byung-Kwan
- Issue Date
- 31-Mar-2015
- Publisher
- OXFORD UNIV PRESS
- Citation
- NUCLEIC ACIDS RESEARCH, v.43, no.6, pp 3079 - 3088
- Pages
- 10
- Indexed
- SCI
SCIE
SCOPUS
- Journal Title
- NUCLEIC ACIDS RESEARCH
- Volume
- 43
- Number
- 6
- Start Page
- 3079
- End Page
- 3088
- URI
- https://scholarworks.dongguk.edu/handle/sw.dongguk/23505
- DOI
- 10.1093/nar/gkv150
- ISSN
- 0305-1048
1362-4962
- Abstract
- DNA-binding motifs that are recognized by transcription factors (TFs) have been well studied; however, challenges remain in determining the in vivo architecture of TF-DNA complexes on a genome-scale. Here, we determined the in vivo architecture of Escherichia coli arginine repressor (ArgR)-DNA complexes using high-throughput sequencing of exonuclease-treated chromatin-immunoprecipitated DNA (ChIP-exo). The ChIP-exo has a unique peak-pair pattern indicating 5' and 3' ends of ArgR-binding region. We identified 62 ArgR-binding loci, which were classified into three groups, comprising single, double and triple peak-pairs. Each peak-pair has a unique 93 base pair (bp)-long (+/- 2 bp) ArgR-binding sequence containing two ARG boxes (39 bp) and residual sequences. Moreover, the three ArgR-binding modes defined by the position of the two ARG boxes indicate that DNA bends centered between the pair of ARG boxes facilitate the non-specific contacts between ArgR subunits and the residual sequences. Additionally, our approach may also reveal other fundamental structural features of TF-DNA interactions that have implications for studying genome-scale transcriptional regulatory networks.
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Collections - College of Engineering > Department of Chemical and Biochemical Engineering > 1. Journal Articles

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