Dynamic interactions of p53 with DNA in solution by time-lapse atomic force microscopy.
Dynamic interactions of the tumor suppressor protein p53 with a DNA fragment containing a p53-specific recognition sequence were directly observed by time-lapse tapping mode atomic force microscopy (AFM) in liquid. The divalent cation Mg(2+) was used to loosely attach both DNA and p53 to a mica surface so they could be imaged by the AFM while interacting with each other. Various interactions of p53 with DNA were observed, including dissociation/re-association, sliding and possibly direct binding to the specific sequence. Two modes of target recognition of p53 were detected: (a) direct binding, and (b) initial non-specific binding with subsequent translocation by one-dimensional diffusion of the protein along the DNA to the specific site.
Jiao
Y
Y
Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Cherny
D I
DI
Heim
G
G
Jovin
T M
TM
Schäffer
T E
TE
D000538:Aluminum Silicates / Q000378:metabolism; D001483:Base Sequence; D002413:Cations, Divalent / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004058:Diffusion; D019281:Dimerization; D006801:Humans; D008274:Magnesium / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D018625:Microscopy, Atomic Force; D009068:Movement; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D020218:Response Elements / Q000235:genetics*; D012996:Solutions; D013379:Substrate Specificity; D013997:Time Factors; D017186:Titrimetry; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism*
D000538:Aluminum Silicates; D002413:Cations, Divalent; D012996:Solutions; D016159:Tumor Suppressor Protein p53; D004247:DNA; D008274:Magnesium; C011934:mica