Protein-DNA interactions under high-pressure conditions, studied by capillary narrow-tube electrophoresis.
The method of electrophoretic mobility shift assay under high-pressure conditions was improved using a high-pressure electrophoresis apparatus with capillary narrow-tube gel. It was found that the protein-DNA complex in the gel was stained as a high-resolution spot with ethidium bromide. Using this method, it was found that the behavior under high-pressure conditions of the protein-DNA complex composed of NtrC protein and its target promoter DNA is important for the pressure-regulated transcription process, and it was confirmed that the complex was dissociated above a pressure of 70 MPa.
Kawano
Hiroaki
H
Extremobiosphere Research Center (XBR), Japan Agency for Marine-Earth Science and Technology (JAMSTEC), 2-15 Natsushima-cho, Yokosuka, Kanagawa 237-0061, Japan. kawanoh@jamstec.go.jp
Nakasone
Kaoru
K
Abe
Fumiyoshi
F
Kato
Chiaki
C
Yoshida
Yasuhiko
Y
Usami
Ron
R
Horikoshi
Koki
K
D001274:Atmospheric Pressure; D001426:Bacterial Proteins / Q000378:metabolism; D004269:DNA, Bacterial / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D019075:Electrophoresis, Capillary / Q000379:methods*; D024202:Electrophoretic Mobility Shift Assay / Q000379:methods*; D011485:Protein Binding; D015203:Reproducibility of Results; D020592:Shewanella / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins