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首页> 外文期刊>Journal of Molecular Biology >GEN1 from a Thermophilic Fungus Is Functionally Closely Similar to Non-Eukaryotic Junction-Resolving Enzymes
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GEN1 from a Thermophilic Fungus Is Functionally Closely Similar to Non-Eukaryotic Junction-Resolving Enzymes

机译：来自嗜热真菌的Gen1在功能上与非真核生物结算酶密切相关

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摘要

Processing of Holliday junctions is essential in recombination. We have identified the gene for the junction-resolving enzyme GEN1 from the thermophilic fungus Chaetomium thermophilum and expressed the N-terminal 487-amino-acid section. The protein is a nuclease that is highly selective for four-way DNA junctions, cleaving 1 nt 3' to the point of strand exchange on two strands symmetrically disposed about a diagonal axis. CtGEN1 binds to DNA junctions as a discrete homodimer with nanomolar affinity. Analysis of the kinetics of cruciform cleavage shows that cleavage of the second strand occurs an order of magnitude faster than the first cleavage so as to generate a productive resolution event. All these properties are closely similar to those described for bacterial, phage and mitochondrial junction-resolving enzymes. CtGEN1 is also similar in properties to the human enzyme but lacks the problems with aggregation that currently prevent detailed analysis of the latter protein. CtGEN1 is thus an excellent enzyme with which to engage in biophysical and structural analysis of eukaryotic GEN1. (C) 2014 MRC Laboratory of Molecular Biology. Published by Elsevier Ltd.
机译：加工Holliday交界处的重组至关重要。我们已经鉴定了从嗜热真菌嗜热嗜热素从嗜热嗜热嗜热嗜热素中鉴定了基因，并表达了N-末端487-氨基酸部分。蛋白质是对对对角线轴对称地设置的两条股线的四元途径交换，将1nt 3'切割1nt 3'的核酸酶。 Ctgen1与具有纳米摩尔亲和力的离散同源聚物结合DNA结合。对十字形切割的动力学分析表明，第二股的切割发生比第一次切割快，以产生生产分辨​​率事件。所有这些性质与细菌，噬菌体和线粒体结溶解酶描述的那些密切相关。 CTGEN1在人酶的性质中也类似，但缺乏具有目前防止后一种蛋白质的详细分析的聚集存在的问题。因此，CTGEN1是一种优异的酶，其与真核基因1的生物物理和结构分析接合。 （c）2014 MRC分子生物学实验室。 elsevier有限公司出版

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