Dynamic interactions of p53 with DNA in solution by time-lapse atomic force microscopy - PubMed (original) (raw)

. 2001 Nov 23;314(2):233-43.

doi: 10.1006/jmbi.2001.5129.

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Dynamic interactions of p53 with DNA in solution by time-lapse atomic force microscopy

Y Jiao et al. J Mol Biol. 2001.

Abstract

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.

Copyright 2001 Academic Press.

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