从嗜堿金属球菌 QYMF 中鉴定一种新型 ArsA ATP 酶复合物的生化特性。
Biochemical characterization of a novel ArsA ATPase complex from Alkaliphilus metalliredigens QYMF.
机构信息
Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, MI 48201, USA.
出版信息
FEBS Lett. 2010 Jul 16;584(14):3089-94. doi: 10.1016/j.febslet.2010.05.044. Epub 2010 May 27.
The two putative ars operons in Alkaliphilus metalliredigens QYMF are distinctive in that the arsA gene is split in halves, amarsA1 and amarsA2, and, acr3 but not an arsB gene coexists with arsA. Heterologous expression of one of the A. metalliredigensars operons (ars1) conferred arsenite but not antimonite resistance to DeltaarsEscherichia coli. Only the co-expressed AmArsA1 and AmArsA2 displayed arsenite or antimonite stimulated ATPase activity. The results show that AmArsA1-AmArsA2 interaction is needed to form the functional ArsA ATPase. This novel AmArsA1-AmArsA2 complex may provide insight in how it participates with Acr3 in arsenite detoxification.
在 Alkaliphilus metalliredigens QYMF 中，两个假定的 ars 操纵子的特点是 arsA 基因被分成两半，即 amarsA1 和 amarsA2，并且 acr3 与 arsA 共存，但没有 arsB 基因。一个 Alkaliphilus metalliredigens ars 操纵子（ars1）的异源表达赋予了 DeltaarsEscherichia coli 对亚砷酸盐而不是锑酸盐的抗性。只有共表达的 AmArsA1 和 AmArsA2 显示出对亚砷酸盐或锑酸盐刺激的 ATP 酶活性。结果表明，AmArsA1-AmArsA2 相互作用是形成功能性 ArsA ATP 酶所必需的。这种新型的 AmArsA1-AmArsA2 复合物可能为了解它如何与 Acr3 一起参与亚砷酸盐解毒提供了线索。
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