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|Title:||A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes||Authors:||Liu, Y.
Heat-stable nucleoid structuring protein (H-NS)
|Issue Date:||15-Feb-2010||Citation:||Liu, Y., Chen, H., Kenney, L.J., Yan, J. (2010-02-15). A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes. Genes and Development 24 (4) : 339-344. ScholarBank@NUS Repository. https://doi.org/10.1101/gad.1883510||Abstract:||Heat-stable nucleoid structuring protein (H-NS) is an abundant prokaryotic protein that plays important roles in organizing chromosomal DNA and gene silencing. Two controversial binding modes were identified. H-NS binding stimulating DNA bridging has become the accepted mechanism, whereas H-NS binding causing DNA stiffening has been largely ignored. Here, we report that both modes exist, and that changes in divalent cations drive a switch between them. The stiffening formis present under physiological conditions, and directly responds to pH and temperature in vitro. Our findings have broad implications and require a reinterpretation of the mechanism by which H-NS regulates genes. © 2010 by Cold Spring Harbor Laboratory Press.||Source Title:||Genes and Development||URI:||http://scholarbank.nus.edu.sg/handle/10635/95618||ISSN:||08909369||DOI:||10.1101/gad.1883510|
|Appears in Collections:||Staff Publications|
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