The architecture of ArgR-DNA complexes at the genome-scale in Escherichia coli

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dc.contributor.authorCho, Suhyungko
dc.contributor.authorCho, Yoo-Bokko
dc.contributor.authorKang, Taek Jinko
dc.contributor.authorKim, Sun Changko
dc.contributor.authorPalsson, Bernhardko
dc.contributor.authorCho, Byung-Kwanko
dc.date.accessioned2015-06-25T06:28:31Z-
dc.date.available2015-06-25T06:28:31Z-
dc.date.created2015-05-13-
dc.date.created2015-05-13-
dc.date.created2015-05-13-
dc.date.issued2015-03-
dc.identifier.citationNUCLEIC ACIDS RESEARCH, v.43, no.6, pp.3079 - 3088-
dc.identifier.issn0305-1048-
dc.identifier.urihttp://hdl.handle.net/10203/199071-
dc.description.abstractDNA-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.-
dc.languageEnglish-
dc.publisherOXFORD UNIV PRESS-
dc.titleThe architecture of ArgR-DNA complexes at the genome-scale in Escherichia coli-
dc.typeArticle-
dc.identifier.wosid000354719300016-
dc.identifier.scopusid2-s2.0-84941746034-
dc.type.rimsART-
dc.citation.volume43-
dc.citation.issue6-
dc.citation.beginningpage3079-
dc.citation.endingpage3088-
dc.citation.publicationnameNUCLEIC ACIDS RESEARCH-
dc.identifier.doi10.1093/nar/gkv150-
dc.contributor.localauthorKim, Sun Chang-
dc.contributor.localauthorCho, Byung-Kwan-
dc.contributor.nonIdAuthorCho, Suhyung-
dc.contributor.nonIdAuthorCho, Yoo-Bok-
dc.contributor.nonIdAuthorKang, Taek Jin-
dc.contributor.nonIdAuthorPalsson, Bernhard-
dc.description.isOpenAccessY-
dc.type.journalArticleArticle-
dc.subject.keywordPlusHEXAMERIC ARGININE REPRESSOR-
dc.subject.keywordPlusBINDING DOMAIN-
dc.subject.keywordPlusOPERATOR INTERACTIONS-
dc.subject.keywordPlusGENE-EXPRESSION-
dc.subject.keywordPlusRNA-POLYMERASE-
dc.subject.keywordPlusH-NS-
dc.subject.keywordPlusPROMOTERS-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordPlusK-12-
dc.subject.keywordPlusREGULON-
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