Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry.
Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry.
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DOI：
10.1016/j.dib.2017.09.068
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发表时间：
2017-12
期刊：
影响因子：
1.2
通讯作者：
Dancis A
中科院分区：
文献类型：
--
作者：
Rocha AG;Knight SAB;Pandey A;Yoon H;Pain J;Pain D;Dancis A
Fe-S团簇是参与多种重要生物过程的辅助因子。线粒体包含一个完整的机器Fe-S簇组装。半胱氨酸脱硫酶（Nfs 1）是产生活性硫所必需的，并且对于最初的Fe-S簇组装步骤是必不可少的。使用质谱法，我们确定了共纯化的蛋白质与Nfs 1使用下拉策略，包括一种新的蛋白激酶。此外，我们能够识别Nfs 1蛋白上的磷酸化位点。这些数据和分析支持罗查等人的研究文章“半胱氨酸脱硫酶受酵母线粒体中Nfs 1磷酸化的调节”（出版中）。
Fe-S clusters are cofactors that participate in diverse and essential biological processes. Mitochondria contain a complete machinery for Fe-S cluster assembly. Cysteine desulfurase (Nfs1) is required generation of a form of activated sulfur and is essential for the initial Fe-S cluster assembly step. Using mass-spectometry we identified proteins that were copurified with Nfs1 using a pull-down strategy, including a novel protein kinase. Furthermore, we were able to identify phosphorylation sites on the Nfs1 protein. These data and analyses support the research article “Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria” by Rocha et al. (in press).