Dürr Harald, Flaus Andrew, Owen-Hughes Tom, Hopfner Karl-Peter
Gene Center, University of Munich, Feodor-Lynen-Strasse 25, D-81377 Munich, Germany.
Nucleic Acids Res. 2006;34(15):4160-7. doi: 10.1093/nar/gkl540. Epub 2006 Aug 25.
Proteins with sequence similarity to the yeast Snf2 protein form a large family of ATPases that act to alter the structure of a diverse range of DNA-protein structures including chromatin. Snf2 family enzymes are related in sequence to DExx box helicases, yet they do not possess helicase activity. Recent biochemical and structural studies suggest that the mechanism by which these enzymes act involves ATP-dependent translocation on DNA. Crystal structures suggest that these enzymes travel along the minor groove, a process that can generate the torque or energy in remodelling processes. We review the recent structural and biochemical findings which suggest a common mechanistic basis underlies the action of many of both Snf2 family and DExx box helicases.
与酵母Snf2蛋白具有序列相似性的蛋白质形成了一个庞大的ATP酶家族,这些酶可改变包括染色质在内的多种DNA-蛋白质结构的结构。Snf2家族酶在序列上与DExx框解旋酶相关,但它们不具备解旋酶活性。最近的生化和结构研究表明,这些酶的作用机制涉及在DNA上的ATP依赖性易位。晶体结构表明,这些酶沿着小沟移动,这一过程可在重塑过程中产生扭矩或能量。我们综述了最近的结构和生化研究结果,这些结果表明许多Snf2家族和DExx框解旋酶的作用都有一个共同的机制基础。