ATP-induced shrinkage of DNA with MukB protein and the MukBEF complex of Escherichia coli.
Fluorescence microscopic observation of individual T4 DNA molecules revealed that the MukBEF complex (bacterial condensin) and its subunit, the MukB (a member of the SMC [structural maintenance of chromosomes] superfamily) homodimer, of Escherichia coli markedly shrunk large DNA molecules in the presence of hydrolyzable ATP. In contrast, in the presence of ADP or ATP-gammaS, the conformation of DNA was almost not changed. This suggests that the ATPase activity of subunit MukB is essential for shrinking large DNA molecules. Stretching experiments on the shrunken DNA molecules in the presence of ATP and MukBEF indicated a cross-bridging interaction between DNA molecules.
Chen
Ning
N
Department of Physics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
Zinchenko
Anatoly A
AA
Yoshikawa
Yuko
Y
Araki
Sumiko
S
Adachi
Shun
S
Yamazoe
Mitsuyoshi
M
Hiraga
Sota
S
Yoshikawa
Kenichi
K
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000187:drug effects / Q000494:pharmacology*; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism; D004269:DNA, Bacterial / Q000737:chemistry / Q000187:drug effects*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000187:drug effects*; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism* / Q000502:physiology*; D008856:Microscopy, Fluorescence; D046912:Multiprotein Complexes / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D012097:Repressor Proteins / Q000378:metabolism
D002868:Chromosomal Proteins, Non-Histone; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C067035:MukB protein, E coli; D046912:Multiprotein Complexes; D012097:Repressor Proteins; C108312:condensin complexes; C087115:mukE protein, E coli; C087116:mukF protein, E coli; D000251:Adenosine Triphosphatases