Dynamic Interactions of P53 with DNA Observed by Time-lapse AFM
Tilman E. Schaffer*, Dmitry I. Cherny, Gudrun Heim, Thomas M. Jovin, and Yuekan Jiao
Molecular Biology Dept., Max Planck Institute for Biophys. Chemistry,
Goettingen 37077 GERMANY
This is an abstract
for a presentation given at the
Ninth
Foresight Conference on Molecular Nanotechnology.
There will be a link from here to the full article when it is
available on the web.
Dynamic interactions of the tumor suppressor protein p53 with a DNA fragment containing a p53-specific consensus sequence were directly observed on a single-molecule basis by time-lapse tapping mode atomic force microscopy (AFM) in liquid. Divalent cations were used to loosely attach both DNA and p53 to a mica surface so they could be imaged by time-lapse AFM while being sufficiently mobile to interact with each other. Various interactions of p53 with DNA were imaged in real-time, 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 nonspecific binding with subsequent translocation by one-dimensional diffusion of the protein along the DNA to the specific site. These results give new insights to the motion of single biomolecules.
*Corresponding Address:
Tilman E. Schaffer
Molecular Biology Dept., Max Planck Institute for Biophys. Chemistry
Am Fassberg 11, Goettingen 37077 GERMANY
Phone: +49 551 201-1762
Fax: +49 551 201-1467
Email: [email protected]
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