Henry Manon, Woods Michael, Gutierrez-Gongora Davier, Geddes-McAlister Jennifer, Sellam Adnane
Montreal Heart Institute/Institut de Cardiologie de Montréal, Université de Montréal, Montreal, QC, Canada.
Department of Microbiology, Infectious Diseases and Immunology, Faculty of Medicine, Université de Montréal, Montreal, QC, Canada.
Data Brief. 2025 Jul 8;61:111862. doi: 10.1016/j.dib.2025.111862. eCollection 2025 Aug.
The ability of the opportunistic yeast to acquire and maintain homeostatic levels of manganese (Mn), particularly in the metal-limited host environment, is an important determinant of its fitness. Although significant focus has been given to mechanisms of iron and copper acquisition and their roles in fitness, little is known about how this yeast maintains and controls Mn homeostasis. Here, we present a comparative proteomic and phosphoproteomic analysis in cells experiencing Mn starvation. Both proteome and phosphoproteome of the reference strain SC5314 grown in Mn-deplete medium were compared to those of cells thriving in Mn-replete medium. Samples were collected in three biological replicates at two time-points (5 and 90 min). Mass spectrometry-based proteomics identified approximately 1500 proteins and over 140 phosphorylated proteins. Proteomic data were analyzed using MaxQuant and Perseus, and all datasets were deposited in the PRIDE repository (accession number PXD064206). Gene ontology analysis was performed to characterize biological processes and signaling pathways affected by Mn availability. This dataset provides a resource for studying Mn homeostasis and regulatory phosphorylation in fungal pathogens. The dataset can be reused for comparative analysis with other fungal species or stress conditions involving transition metal availability.
这种机会性酵母获取并维持锰(Mn)稳态水平的能力,尤其是在金属受限的宿主环境中,是其适应性的一个重要决定因素。尽管人们已大量关注铁和铜的获取机制及其在适应性方面的作用,但对于这种酵母如何维持和控制锰稳态却知之甚少。在此,我们对经历锰饥饿的细胞进行了比较蛋白质组学和磷酸化蛋白质组学分析。将在缺锰培养基中生长的参考菌株SC5314的蛋白质组和磷酸化蛋白质组与在锰充足培养基中茁壮生长的细胞的蛋白质组和磷酸化蛋白质组进行了比较。在两个时间点(5分钟和90分钟)收集了三个生物学重复的样本。基于质谱的蛋白质组学鉴定出了大约1500种蛋白质和140多种磷酸化蛋白质。使用MaxQuant和Perseus对蛋白质组学数据进行了分析,所有数据集都存放在PRIDE数据库中(登录号PXD064206)。进行了基因本体分析,以表征受锰可用性影响的生物学过程和信号通路。该数据集为研究真菌病原体中的锰稳态和调节性磷酸化提供了资源。该数据集可重新用于与其他真菌物种或涉及过渡金属可用性的应激条件进行比较分析。