Quantitative proteomics analysis reveals alterations of lysine acetylation in mouse testis in response to heat shock and X-ray exposure
Quantitative proteomics analysis reveals alterations of lysine acetylation in mouse testis in response to heat shock and X-ray exposure
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定量蛋白质组学分析揭示了小鼠睾丸中赖氨酸乙酰化因热休克和 X 射线暴露而发生的变化
DOI：
10.1016/j.bbapap.2017.11.011
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发表时间：
2018
影响因子：
3.2
通讯作者：
Guo Caixia
中科院分区：
文献类型：
--
作者：
Xie Chengmei;Shen Hongyan;Zhang Hui;Yan Jinting;Liu Yang;Yao Fuwen;Wang Xi;Cheng Zhongyi;Tang Tie-Shan;Guo Caixia
环境应激是引起男性不育的重要因素，引起了广泛关注。蛋白质乙酰化是一种重要的翻译后修饰，调节包括精子发生在内的多种生理过程。本研究利用定量蛋白质组学技术和生物信息学工具，分析了热休克和X射线照射后小鼠睾丸乙酰组的变化。总的来说，我们确定了1139赖氨酸乙酰化位点在587个蛋白质，其中1020赖氨酸乙酰化位点进行了定量。基因本体分析表明，主要的乙酰化蛋白质组参与前体代谢产物的产生和代谢过程，并且主要定位于细胞溶质和线粒体中。与对照组相比，28个乙酰化蛋白质中有36个位点在热休克后发生了变化，43个乙酰化蛋白质中有49个位点在X射线照射后发生了变化。一些差异乙酰化的蛋白质已被报道与精子发生和男性生育力的进展。我们观察到睾丸特异性组蛋白2B和热休克蛋白的乙酰化水平在热处理后上调，而组蛋白H2AX的乙酰化水平在X射线处理后急剧下降，表明它们在雄性生殖细胞中的作用。值得注意的是，组蛋白乙酰转移酶（Kat7）K279的乙酰化水平在热和X射线处理下调，表明K279可能是一个关键的乙酰化位点，并影响其在精子发生中的功能。我们的研究结果表明，蛋白质乙酰化可能增加了另一层复杂的调控精子发生，这些蛋白质的功能的进一步研究将有助于我们阐明异常精子发生的机制。
Environmental stresses are important factors causing male infertility which attracts broad attention. Protein acetylation is a pivotal post-translational modification and modulates diverse physiological processes including spermatogenesis. In this study, we employed quantitative proteomic techniques and bioinformatics tools to analyze the alterations of acetylome profile of mouse testis after heat shock and X-irradiation. Overall, we identified 1139 lysine acetylation sites in 587 proteins in which 1020 lysine acetylation sites were quantified. The Gene Ontology analysis showed that the major acetylated protein groups were involved in generation of precursor metabolites and metabolic processes, and were localized predominantly in cytosolic and mitochondrial. Compared to the control group, 36 sites of 28 acetylated proteins have changed after heat shock, and 49 sites of 43 acetylated proteins for X-ray exposure. Some of the differentially acetylated proteins have been reported to be associated with the progression of spermatogenesis and male fertility. We observed the up-regulated acetylation level change on testis specific histone 2B and heat shock protein upon heat treatment and a sharp decline of acetylation level on histone H2AX under X-ray treatment, suggesting their roles in male germ cells. Notably, the acetylation level on K279 of histone acetyltransferase (Kat7) was down-regulated in both heat and X-ray treatments, indicating that K279 may be a key acetylated site and affect its functions in spermatogenesis. Our results reveal that protein acetylation might add another layer of complexity to the regulation for spermatogenesis, and further functional studies of these proteins will help us elucidate the mechanisms of abnormal spermatogenesis.