Klysik J, Shimizu M
Department of Biochemistry, School of Medicine, University of Alabama at Birmingham 35294.
FEBS Lett. 1993 Nov 1;333(3):261-7. doi: 10.1016/0014-5793(93)80666-i.
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.
评估了大肠杆菌单链DNA结合蛋白（SSB）识别与寡嘌呤-寡嘧啶（pur.pyr）插入重组质粒中分子内三链体形成相关结构特征的能力。SSB蛋白与超螺旋质粒结合，并导致参与三链体结构Hy-3异构体形成的嘧啶链的OsO4反应性出现位点优先增加。在类似研究中，大肠杆菌RecA蛋白与三链体无反应。这种行为与SSB介导的H-DNA形成区域的解配对一致。
