West S C, Cassuto E, Howard-Flanders P
Nature. 1981 Mar 5;290(5801):29-33. doi: 10.1038/290029a0.
In the presence of ATP and Mg2+, purified Escherichia coli recA protein promotes the formation of joint molecules between closed circular duplex DNA and homologous circular single-stranded DNA carrying a short annealed fragment. The presence of this fragment is essential for pairing between molecules. In similar conditions recA protein is unable to act as a helicase and does not cause strand separation of the fragment from the single-stranded circle. Thus, homologous pairing between DNA molecules can take place without prior unwinding of a free end.
在ATP和Mg2+存在的情况下,纯化的大肠杆菌recA蛋白可促进封闭环状双链DNA与携带短退火片段的同源环状单链DNA之间形成连接分子。该片段的存在对于分子间的配对至关重要。在类似条件下,recA蛋白不能作为解旋酶起作用,也不会导致片段与单链环的链分离。因此,DNA分子之间的同源配对可以在没有自由末端预先解旋的情况下发生。