Escherichia coli single-stranded DNA-binding protein alters the structure of intramolecular triplexes in plasmids

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Abstract

The ability of the Escherichia coli single-stranded DNA-binding protein (SSB) to recognize structural features associated with intramolecular triplex formation in oligopurine · oligopyrimidine (pur · pyr) inserts in recombinant plasmids was evaluated. The SSB protein binds to supercoiled plasmids and causes a site-preferential increase in OsO4 reactivity of the pyrimidine strand involved in the formation of the Hy-3 isomer of the triplex structure. The E. coli RecA protein showed no reaction with triplexes in similar studies. This behavior is consistent with SSB-mediated unpairing of the H-DNA-forming region. © 1993.

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Klysik, J., & Shimizu, M. (1993). Escherichia coli single-stranded DNA-binding protein alters the structure of intramolecular triplexes in plasmids. FEBS Letters, 333(3), 261–267. https://doi.org/10.1016/0014-5793(93)80666-I

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