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首页> 外文期刊>Journal of Molecular Biology >DNA binding and cleavage by the HNH homing endonuclease I-Hmul
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DNA binding and cleavage by the HNH homing endonuclease I-Hmul

机译：HNH归巢内切核酸酶I-Hmul对DNA的结合和切割

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摘要

The structure of I-HmuI, which represents the last family of homing endonucleases without a defining crystallographic structure, has been determined in complex with its DNA target. A series of diverse protein structural domains and motifs, contacting sequential stretches of nucleotide bases, are distributed along the DNA target. I-HmuI contains an N-terminal domain with a DNA-binding surface found in the I-PpoI homing endonuclease and an associated HNH/N active site found in the bacterial colicins, and a C-terminal DNA-binding domain previously observed in the I-TevI homing endonuclease. The combination and exchange of these features between protein families indicates that the genetic mobility associated with homing endonucleases extends to the level of independent structural domains. I-HmuI provides an unambiguous structural connection between the His-Cys box endonucleases and the bacterial colicins, supporting the hypothesis that these enzymes diverged from a common ancestral nuclease. (C) 2004 Elsevier Ltd. All rights reserved.
机译：I-HmuI的结构代表了归巢核酸内切酶的最后一个家族，但没有确定的晶体学结构，已与其DNA靶标复合确定。一系列不同的蛋白质结构域和基序，与核苷酸碱基的连续序列接触，沿着DNA靶标分布。 I-HmuI包含一个在I-PpoI归巢核酸内切酶中发现的具有DNA结合表面的N末端结构域和一个在细菌大肠菌素中发现的相关HNH / N活性位点，以及一个在C-末端的C-末端DNA结合结构域。 I-TevI​​归巢核酸内切酶。蛋白质家族之间这些特征的组合和交换表明与归巢核酸内切酶相关的遗传迁移性扩展到独立结构域的水平。 I-HmuI在His-Cys盒内切核酸酶和细菌大肠菌素之间提供了明确的结构连接，支持了这些酶与普通祖先核酸酶不同的假设。 （C）2004 Elsevier Ltd.保留所有权利。

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