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Escherichia coli single‐stranded DNA‐binding protein alters the structure of intramolecular triplexes in plasmids
Author(s) -
Klysik Jan,
Shimizu Mitsuhiro
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80666-i
Subject(s) - escherichia coli , plasmid , dna , recombinant dna , intramolecular force , chemistry , biophysics , biology , microbiology and biotechnology , biochemistry , stereochemistry , gene
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 OsO 4 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.