Please use this identifier to cite or link to this item: https://doi.org/10.1038/srep18146
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dc.titleRegulation of Bacterial DNA Packaging in Early Stationary Phase by Competitive DNA Binding of Dps and IHF
dc.contributor.authorLee, S.Y
dc.contributor.authorLim, C.J
dc.contributor.authorDr”ge, P
dc.contributor.authorYan, J
dc.date.accessioned2020-09-14T07:34:29Z
dc.date.available2020-09-14T07:34:29Z
dc.date.issued2015
dc.identifier.citationLee, S.Y, Lim, C.J, Dr”ge, P, Yan, J (2015). Regulation of Bacterial DNA Packaging in Early Stationary Phase by Competitive DNA Binding of Dps and IHF. Scientific Reports 5 : 18146. ScholarBank@NUS Repository. https://doi.org/10.1038/srep18146
dc.identifier.issn2045-2322
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/175972
dc.description.abstractThe bacterial nucleoid, a bacterial genome packed by nucleoid binding proteins, forms the physical basis for cellular processes such as gene transcription and DNA replication. Bacteria need to dynamically modulate their nucleoid structures at different growth phases and in response to environmental changes. At the nutrients deficient stationary phase, DNA-binding proteins from starved cells (Dps) and Integration host factors (IHF) are the two most abundant nucleoid associated proteins in E. coli. Yet, it remains unclear how the nucleoid architecture is controlled by the interplay between these two proteins, as well as the nucleoid's response to environmental changes. This question is addressed here using single DNA manipulation approach. Our results reveal that the two proteins are differentially selected for DNA binding, which can be tuned by changing environmental factors over physiological ranges including KCl (50-300 mM), MgCl2 (0-10 mM), pH (6.5-8.5) and temperature (23-37 шC). Increasing pH and MgCl2 concentrations switch from Dps-binding to IHF-binding. Stable Dps-DNA and IHF-DNA complexes are insensitive to temperature changes for the range tested. The environment dependent selection between IHF and Dps results in different physical organizations of DNA. Overall, our findings provide important insights into E. coli nucleoid architecture.
dc.sourceUnpaywall 20200831
dc.subjectbacterial DNA
dc.subjectDNA binding protein
dc.subjectEscherichia coli protein
dc.subjectintegration host factor
dc.subjectmagnesium chloride
dc.subjectpotassium chloride
dc.subjectprotein binding
dc.subjectbacterial genome
dc.subjectbinding competition
dc.subjectDNA packaging
dc.subjectdrug effects
dc.subjectEscherichia coli
dc.subjectgene expression regulation
dc.subjectgenetics
dc.subjectgrowth, development and aging
dc.subjectmagnetism
dc.subjectmetabolism
dc.subjectoptical tweezers
dc.subjectpH
dc.subjectBinding, Competitive
dc.subjectDNA Packaging
dc.subjectDNA, Bacterial
dc.subjectDNA-Binding Proteins
dc.subjectEscherichia coli
dc.subjectEscherichia coli Proteins
dc.subjectGene Expression Regulation, Bacterial
dc.subjectGenome, Bacterial
dc.subjectHydrogen-Ion Concentration
dc.subjectIntegration Host Factors
dc.subjectMagnesium Chloride
dc.subjectMagnetics
dc.subjectOptical Tweezers
dc.subjectPotassium Chloride
dc.subjectProtein Binding
dc.typeArticle
dc.contributor.departmentPHYSICS
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.description.doi10.1038/srep18146
dc.description.sourcetitleScientific Reports
dc.description.volume5
dc.description.page18146
dc.published.statePublished
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