期刊
GENES & DEVELOPMENT
卷 24, 期 4, 页码 339-344出版社
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1883510
关键词
Heat-stable nucleoid structuring protein (H-NS); gene silencing; transcriptional regulation; pathogenicity islands; atomic force microscopy; magnetic tweezers
资金
- National Institutes of Health [GM-058746]
- Veterans Administration [1I01BX000372]
- Ministry of Education of Singapore [R144000192112, R144000251112]
- Mechanobiology Program at the National University of Singapore
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据