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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Klysik J,Shimizu Mdoi
10.1016/0014-5793(93)80666-isubject
Has Abstractpub_date
1993-11-01 00:00:00pages
261-7issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(93)80666-Ijournal_volume
333pub_type
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