The PX Motif of DNA Binds Specifically to Escherichia coli DNA Polymerase i

Xiang Gao, Matthew Gethers, Si Ping Han, William A. Goddard, Ruojie Sha, Richard P. Cunningham, Nadrian C. Seeman

Research output: Contribution to journalArticle

Abstract

The PX motif of DNA is a four-stranded structure in which two parallel juxtaposed double-helical domains are fused by crossovers at every point where the strands approach each other. Consequently, its twist and writhe are approximately half of those of conventional DNA. This property has been shown to relax supercoiled plasmid DNA under circumstances in which head-to-head homology exists within the plasmid; the homology can be either complete homology or every-other-half-turn homology, known as PX homology. It is clearly of interest to establish whether the cell contains proteins that interact with this unusual and possibly functional motif. We have examined Escherichia coli extracts to seek such a protein. We find by gel mobility studies that the PX motif is apparently bound by a cellular component. Fractionation of this binding activity reveals that the component is DNA polymerase I (Pol I). Although the PX motif binds to Pol I, we find that PX-DNA is not able to serve as a substrate for the extension of a shortened strand. We cannot say at this time whether the binding is a coincidence or whether it represents an activity of Pol I that is currently unknown. We have modeled the interaction of Pol I and PX-DNA using symmetry considerations and molecular dynamics.

Original languageEnglish (US)
Pages (from-to)575-581
Number of pages7
JournalBiochemistry
Volume58
Issue number6
DOIs
StatePublished - Feb 12 2019

ASJC Scopus subject areas

  • Biochemistry

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