大肠杆菌 slyD，不只是镍(II)储存器。
Escherichia coli SlyD, more than a Ni(II) reservoir.
机构信息
Department of Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 3H6.
出版信息
Biochemistry. 2011 Dec 20;50(50):10761-3. doi: 10.1021/bi201590d. Epub 2011 Nov 18.
Abstract
SlyD interacts with HypB and contributes to nickel insertion during [NiFe]-hydrogenase biogenesis. Herein, we provide evidence of SlyD acting as a nickel storage determinant in Escherichia coli and show that this Ni(II) can be mobilized to HypB in vitro even under competitive conditions. Furthermore, SlyD enhances the GTPase activity of HypB, and acceleration of release of Ni(II) from HypB is more pronounced when HypB is GDP-bound. The data support a model in which a HypB-SlyD complex establishes communication between GTP hydrolysis and nickel delivery and provide insight into the role of the HypB-SlyD complex during [NiFe]-hydrogenase biosynthesis.
摘要
SlyD 与 HypB 相互作用，并有助于 [NiFe]-氢化酶生物发生过程中的镍插入。在此，我们提供了 SlyD 作为大肠杆菌中镍储存决定因素的证据，并表明即使在竞争条件下，这种 Ni(II)也可以在体外转移到 HypB。此外，SlyD 增强了 HypB 的 GTPase 活性，并且当 HypB 与 GDP 结合时，从 HypB 释放 Ni(II)的速度更快。这些数据支持了一个模型，即 HypB-SlyD 复合物在 GTP 水解和镍传递之间建立了通讯，并深入了解了 HypB-SlyD 复合物在 [NiFe]-氢化酶生物合成过程中的作用。
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本文引用的文献
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Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase.大肠杆菌辅助蛋白 HypA 在镍插入 [NiFe] 氢化酶过程中的蛋白相互作用和定位。
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