Lapkouski Mikalai, Panjikar Santosh, Janscak Pavel, Smatanova Ivana Kuta, Carey Jannette, Ettrich Rüdiger, Csefalvay Eva
Department of Structure and Function of Proteins, Institute of Systems Biology and Ecology, Academy of Sciences of the Czech Republic, Nove Hrady, Czech Republic.
Nat Struct Mol Biol. 2009 Jan;16(1):94-5. doi: 10.1038/nsmb.1523. Epub 2008 Dec 14.
Type I restriction-modification enzymes act as conventional adenine methylases on hemimethylated DNAs, but unmethylated recognition targets induce them to translocate thousands of base pairs before cleaving distant sites nonspecifically. The first crystal structure of a type I motor subunit responsible for translocation and cleavage suggests how the pentameric translocating complex is assembled and provides a structural framework for translocation of duplex DNA by RecA-like ATPase motors.
I 型限制-修饰酶在半甲基化 DNA 上作为常规腺嘌呤甲基化酶起作用,但未甲基化的识别靶点会诱导它们在非特异性切割远处位点之前移位数千个碱基对。负责移位和切割的 I 型运动亚基的首个晶体结构揭示了五聚体移位复合物是如何组装的,并为双链 DNA 通过 RecA 样 ATP 酶马达进行移位提供了结构框架。