Please use this identifier to cite or link to this item:
|Title:||The nucleoid-associated protein Dan organizes chromosomal DNA through rigid nucleoprotein filament formation in E. coli during anoxia|
|Citation:||Lim, C.J., Lee, S.Y., Teramoto, J., Ishihama, A., Yan, J. (2013-01). The nucleoid-associated protein Dan organizes chromosomal DNA through rigid nucleoprotein filament formation in E. coli during anoxia. Nucleic Acids Research 41 (2) : 746-753. ScholarBank@NUS Repository. https://doi.org/10.1093/nar/gks1126|
|Abstract:||Dan is a transcription factor that regulates the ttd operon encoding tartrate dehydratase. During anaerobic conditions, its copy number increases by 100-fold, making Dan an abundant nucleoid-associated protein. However, little is known about the mode of Dan-DNA interaction. To understand its cellular functions, we used single-molecule manipulation and imaging techniques to show that Dan binds cooperatively along DNA, resulting in formation of a rigid periodic nucleoprotein filament that strongly restricts accessibility to DNA. Furthermore, in the presence of physiologic levels of magnesium, these filaments interact with each other to cause global DNA condensation. Overall, these results shed light on the architectural role of Dan in the compaction of Escherichia coli chromosomal DNA under anaerobic conditions. Formation of the nucleoprotein filament provides a basis in understanding how Dan may play roles in both chromosomal DNA protection and gene regulation. © 2012 The Author(s).|
|Source Title:||Nucleic Acids Research|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Oct 18, 2018
WEB OF SCIENCETM
checked on Oct 2, 2018
checked on Oct 5, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.