Biochemical, molecular genetic, and structural analyses of the staphylococcal nucleoid.
The nucleoid structure of an important human pathogen, Staphylococcus aureus, was dissected by atomic force microscopy (AFM). The nucleoids dispersed on a cover glass consisted of fibrous units with two different widths of 40 and 80 nm, a feature shared with those of Escherichia coli. On the other hand, cells exposed to an oxidative stress exhibited clogged nucleoids. A knock-out of mrgA (metallo regulated genes A) encoding a staphylococcal homolog of the nucleoid compaction factor (E. coli Dps) eliminated the compaction response to the oxidative stress and reduced the susceptibilities to H2O2 and UV irradiation. We also observed that the negative supercoiling of plasmids is increased by the oxidative stress. A possible interrelation between the helical density and the nucleoid compaction is discussed in relation to the oxidative stress response.
Morikawa
Kazuya
K
Institute of Basic Medical Sciences, Graduate School of Comprehensive Human Sciences, University of Tsukuba, Tennoh-dai, Tsukuba 305-8575, Japan. morikawa@sakura.cc.tsukuba.ac.jp
Ohniwa
Ryosuke L
RL
Kim
Joongbaek
J
Takeshita
Sayaka L
SL
Maruyama
Atsushi
A
Inose
Yumiko
Y
Takeyasu
Kunio
K
Ohta
Toshiko
T
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D004269:DNA, Bacterial / Q000235:genetics / Q000378:metabolism; D004278:DNA, Superhelical / Q000235:genetics / Q000378:metabolism; D016680:Genome, Bacterial / Q000235:genetics* / Q000528:radiation effects; D018625:Microscopy, Atomic Force / Q000379:methods; D013211:Staphylococcus aureus / Q000235:genetics* / Q000378:metabolism / Q000528:radiation effects; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004278:DNA, Superhelical