H-NS promotes looped domain formation in the bacterial chromosome.
The bacterial chromosome is organized into loops, which constitute topologically isolated domains. It is unclear which proteins are responsible for the formation of the topological barriers between domains. The abundant DNA-binding histone-like nucleoid structuring protein (H-NS) is a key player in the organization and compaction of bacterial chromosomes [1,2]. The protein acts by bridging DNA duplexes [3], thus allowing for the formation of DNA loops. Here, genome-wide studies of H-NS binding suggest that this protein is directly involved in the formation or maintenance of topological domain barriers.
Noom
Maarten C
MC
Navarre
William W
WW
Oshima
Taku
T
Wuite
Gijs J L
GJ
Dame
Remus T
RT
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002876:Chromosomes, Bacterial / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D012486:Salmonella typhimurium / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C031908:H-NS protein, bacteria