Hotta Y, Stern H
Biochemistry. 1978 May 16;17(10):1872-80. doi: 10.1021/bi00603a011.
An ATP-dependent DNA unwinding protein is present at a high level of activity in meiotic cells of lilies. The protein also acts as a DNA-dependent ATPase, the single strand form being the preferred cofactor. It binds in the absence of ATP to single-strand DNA and to ends or nicks in duplex DNA. A 3'-OH terminus is required for binding at duplex ends; such binding is highly stable. Unwinding occurs in the presence of ATP, and it is limited to about 50 base pairs per end or 400-500 base pairs per nick. The ATP hydrolyzed during unwinding is distinguishable from ATP hydrolysis in the presence of single-strand DNA.
一种依赖ATP的DNA解旋蛋白在百合减数分裂细胞中具有高水平的活性。该蛋白还作为一种依赖DNA的ATP酶，单链形式是其首选辅因子。在没有ATP的情况下，它会与单链DNA以及双链DNA的末端或切口结合。在双链末端结合需要一个3'-OH末端；这种结合非常稳定。在ATP存在的情况下会发生解旋，并且每端限于约50个碱基对或每个切口限于400-500个碱基对。解旋过程中水解的ATP与单链DNA存在时的ATP水解是有区别的。
