蛋白磷酸酶-1 活性位点的自发金属负载和伴侣辅助金属负载。

IF 3.5 4区 生物学 Q1 Biochemistry, Genetics and Molecular Biology FEBS Letters Pub Date : 2024-09-08 DOI:10.1002/1873-3468.15012
Gerd Van der Hoeven, Sarah Lemaire, Xinyu Cao, Zander Claes, Spyridoula Karamanou, Mathieu Bollen
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摘要

蛋白磷酸酶 PP1 有两个活性位点金属(Zn2+/Fe2+),是催化所必需的。然而,在细菌中表达时,PP1 的活性位点有两个 Mn2+离子,这表明 Zn2+/Fe2+的掺入取决于额外的真核成分。在这里,我们使用纯化的、金属缺陷的 PP1 来研究金属的掺入。Fe2+能自发掺入,但Zn2+不能。Mn2+在生理pH值下的掺入取决于PP1与PPP1R2(抑制剂-2)或PPP1R11(抑制剂-3)的共表达,或PP1在pH值为4时的预孵育。 我们还证明,PPP1R2和PPP1R11是Zn2+结合蛋白,但它们本身不能用Zn2+负载PP1。我们的数据表明,PPP1R2 和 PPP1R11 起着 PP1 金属伴侣的作用,但要将相关的 Zn2+ 转移到 PP1 上,还需要辅助伴侣和/或特定修饰。
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Spontaneous and chaperone-assisted metal loading in the active site of protein phosphatase-1.

Protein phosphatase PP1 has two active-site metals (Zn2+/Fe2+) that are essential for catalysis. However, when expressed in bacteria, PP1 has two Mn2+-ions in its active site, indicating that the incorporation of Zn2+/Fe2+ depends on additional eukaryotic component(s). Here, we used purified, metal-deficient PP1 to study metal incorporation. Fe2+ was incorporated spontaneously, but Zn2+ was not. Mn2+-incorporation at physiological pH depended on the co-expression of PP1 with PPP1R2 (Inhibitor-2) or PPP1R11 (Inhibitor-3), or a pre-incubation of PP1 at pH 4. We also demonstrate that PPP1R2 and PPP1R11 are Zn2+-binding proteins but are, by themselves, not able to load PP1 with Zn2+. Our data suggest that PPP1R2 and PPP1R11 function as metal chaperones for PP1 but depend on co-chaperone(s) and/or specific modification(s) for the transfer of associated Zn2+ to PP1.

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来源期刊
FEBS Letters
FEBS Letters 生物-生化与分子生物学
CiteScore
7.00
自引率
2.90%
发文量
303
审稿时长
1.0 months
期刊介绍: FEBS Letters is one of the world''s leading journals in molecular biology and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, Research Letters and Hypotheses that merit urgent publication.
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