MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes
MlaA, a hexameric ATPase linked to the Mre11 complex in archaeal genomes
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DOI：
10.1038/sj.embor.7400037
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发表时间：
2004-01-01
期刊：
影响因子：
7.7
通讯作者：
Hopfner, KP
中科院分区：
文献类型：
--
作者：
Manzan, A;Pfeiffer, G;Hopfner, KP
我们鉴定并表征了 MlaA，一种新型蛋白质，它存在于古细菌基因组中具有 Mre11 和 Rad50 的保守操纵子中。 MlaA 在嗜热自养甲烷杆菌中与 Mre11 融合，表明 MlaA 在功能上与 Mre11 复合体相连。 MlaA 优先并协同地结合双链和含有二级结构的 DNA，并具有双链而非单链 DNA 刺激的 ATP 酶活性。电子显微镜显示 MlaA 形成具有中心孔的 360 kDa 六聚环结构。我们的数据表明，古细菌 Mre11 复合物与一种新型六聚体 ATP 酶相关，这种酶可能是处理 DNA 双链断裂和重组中间体所必需的。
We identify and characterize MlaA, a novel protein, which is found in a conserved operon with Mre11 and Rad50 in archaeal genomes. MlaA is fused with Mre11 in Methanobacter thermoautotrophicus, suggesting the MlaA is functionally linked to the Mre11 complex. MlaA preferentially and cooperatively binds double-stranded and secondary structure containing DNA and has double-stranded but not single-stranded DNA-stimulated ATPase activity. Electron microscopy reveals that MlaA forms a 360-kDa hexameric ring structure with a central hole. Our data suggest that the archaeal Mre11 complex is associated with a novel hexameric ATPase that could be required for the processing of DNA double-stranded breaks and recombination intermediates.