分析溶组织内阿米巴的蛋白质磷酸组揭示了一个错综复杂的磷酸化网络。
Analysis of the Protein phosphotome of Entamoeba histolytica reveals an intricate phosphorylation network.
机构信息
School of Life Sciences, Jawaharlal Nehru University, New Delhi, India.
出版信息
PLoS One. 2013 Nov 13;8(11):e78714. doi: 10.1371/journal.pone.0078714. eCollection 2013.
Phosphorylation is the most common mechanism for the propagation of intracellular signals. Protein phosphatases and protein kinases play a dynamic antagonistic role in protein phosphorylation. Protein phosphatases make up a significant fraction of eukaryotic proteome. In this article, we report the identification and analysis of protein phosphatases in the intracellular parasite Entamoeba histolytica. Based on an in silico analysis, we classified 250 non-redundant protein phosphatases in E. histolytica. The phosphotome of E. histolytica is 3.1% of its proteome and 1.3 times of the human phosphotome. In this extensive study, we identified 42 new putative phosphatases (39 hypothetical proteins and 3 pseudophosphatases). The presence of pseudophosphatases may have an important role in virulence of E. histolytica. A comprehensive phosphotome analysis of E. histolytica shows spectacular low similarity to human phosphatases, making them potent candidates for drug target.
磷酸化是细胞内信号传递最普遍的机制。蛋白磷酸酶和蛋白激酶在蛋白磷酸化中起着动态拮抗的作用。蛋白磷酸酶构成了真核生物蛋白质组的重要组成部分。在本文中，我们报道了内阿米巴原虫中蛋白磷酸酶的鉴定和分析。基于计算机分析，我们在溶组织内阿米巴中鉴定了 250 个非冗余的蛋白磷酸酶。溶组织内阿米巴的磷酸组占其蛋白质组的 3.1%，是人类磷酸组的 1.3 倍。在这项广泛的研究中，我们鉴定了 42 种新的假定磷酸酶（39 种假设蛋白和 3 种假磷酸酶）。假磷酸酶的存在可能在溶组织内阿米巴的毒力中起重要作用。溶组织内阿米巴的磷酸组分析表明与人类磷酸酶的相似度极低，这使它们成为药物靶点的有力候选者。
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