Domain organization and metal ion requirement of the Type IIS restriction endonuclease MnlI
Domain organization and metal ion requirement of the Type IIS restriction endonuclease MnlI
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DOI：
10.1016/j.febslet.2006.09.075
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发表时间：
2006-11-13
期刊：
影响因子：
3.5
通讯作者：
Kriukiene, Edita
中科院分区：
文献类型：
--
作者：
Kriukiene, Edita
US型限制性内切核酸酶穆尔的双结构域结构已通过有限的蛋白水解鉴定。酶的N-末端结构域介导与DNA的序列特异性相互作用，而单体C-末端结构域类似于细菌大肠杆菌素核酸酶，其需要碱土金属以及过渡金属离子用于双链和单链DNA切割活性。结果表明，非特异性HNH型核酸酶与DNA结合结构域的融合将穆尔转化为Mg 2 +-，Ni 2 +-，Co 2 +-，Mn 2 +-，Zn 2 +-，Ca 2 +-依赖的序列特异性酶。然而，穆尔保留了由其C-末端大肠杆菌素样核酸酶结构域控制的残余单链DNA切割活性。(c)2006年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
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.