期刊
FEBS LETTERS
卷 580, 期 26, 页码 6115-6122出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.09.075
关键词
restriction endonuclease; HNH motif; colicin; modular structure; MnlI
A two-domain structure of the Type US restriction endonuclease Mull has been identified by limited proteolysis. An N-terminal domain of the enzyme mediates the sequence-specific interaction with DNA, whereas a monomeric C-terminal domain resembles bacterial colicin nucleases in its requirement for alkaline earth as well as transition metal ions for double- and single-stranded DNA cleavage activities. The results indicate that the fusion of the non-specific HNH-type nuclease to the DNA binding domain had transformed Mull into a Mg2+-, Ni2+-, Co2+-, Mn2+-, Zn2+-, Ca2+-dependent sequence-specific enzyme. Nevertheless, Mull retains a residual single-stranded DNA cleavage activity controlled by its C-terminal colicin-like nuclease domain. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据