Lasken R S, Kornberg A
Department of Biochemistry, Stanford University School of Medicine, California 94305.
J Biol Chem. 1988 Apr 25;263(12):5512-8.
Protein n' of Escherichia coli functions in assembly and translocation of the primosome, a mobile multiprotein complex involved in priming DNA replication (Kornberg, A. (1982) Supplement to DNA Replication, Freeman Publications, San Francisco). By itself, protein n' translocates on single-stranded DNA and destabilizes duplex regions by acting as a DNA helicase, using the energy of ATP or dATP hydrolysis. Single-stranded DNA binding protein was required for melting of duplex regions longer than 40 base pairs. Initial binding of protein n' to a specific site on DNA (Shlomai, J., and Kornberg, A. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 799-803) is essential for its helicase function. The polarity of protein n' translocation on DNA, in the 3' to 5' direction of the chain, suggests a mechanism for how the primosome may contribute to concurrent replication of both strands at a replication fork.
大肠杆菌的蛋白质n'在引发体的组装和移位过程中发挥作用，引发体是一种参与启动DNA复制的移动多蛋白复合体（科恩伯格，A.（1982年）《DNA复制补编》，弗里曼出版社，旧金山）。蛋白质n'自身能在单链DNA上移位，并通过充当DNA解旋酶，利用ATP或dATP水解产生的能量使双链区域不稳定。对于长度超过40个碱基对的双链区域的解链，需要单链DNA结合蛋白。蛋白质n'最初与DNA上的特定位点结合（什洛迈，J.，和科恩伯格，A.（1980年）《美国国家科学院院刊》77，799 - 803）对其解旋酶功能至关重要。蛋白质n'在DNA上沿链的3'至5'方向移位的极性，提示了引发体可能如何在复制叉处对两条链的同时复制起作用的一种机制。
