Protein intrinsic disorder within the Potyvirus genus: from proteome-wide analysis to functional annotation
Protein intrinsic disorder within the Potyvirus genus: from proteome-wide analysis to functional annotation
复制标题
DOI：
10.1039/c5mb00677e
复制
发表时间：
2016-01-01
影响因子：
--
通讯作者：
Michon, Thierry
中科院分区：
文献类型：
--
作者：
Charon, Justine;Theil, Sebastien;Michon, Thierry
在蛋白质内，内在无序区（IDR）在生理条件下缺乏稳定的二级和三级结构，而是作为相互转换构象异构体的动态集合而存在。虽然在生命的所有领域中普遍存在，但内在的疾病内容在病毒基因组中是高度可变的。多年来，在整个蛋白质组的规模无序区域的功能注释已经进行了几种动物病毒。但到目前为止，应用于植物病毒的类似研究仍然缺失。基于无序预测工具结合注释程序和进化研究，我们分析了Potyvirus中的内在无序内容，使用代表该属多样性的10种数据集。在本文中，我们发现：（i）马铃薯Y病毒蛋白质组显示出高的无序内容，（ii）在马铃薯Y病毒进化过程中，无序是保守的，这表明IDRs的功能优势，（iii）IDRs比有序区域进化得更快，（iv）IDRs可能与马铃薯Y病毒周期所需的主要生物学功能相关。值得注意的是，蛋白质P1，外壳蛋白（CP）和病毒基因组连接蛋白（VPg）显示出高含量的保守性疾病，富含模拟真核生物功能模块的特定基序，并暗示宿主机器劫持的策略。在这三种蛋白质中，IDR尽管具有高氨基酸多态性，但特别保守，表明与适应过程有关。通过这项全面的研究，我们进一步研究了马铃薯Y病毒生物学中内在紊乱的生物学相关性，并提出了马铃薯Y病毒蛋白质组IDRs的功能注释。
Within proteins, intrinsically disordered regions (IDRs) are devoid of stable secondary and tertiary structures under physiological conditions and rather exist as dynamic ensembles of inter-converting conformers. Although ubiquitous in all domains of life, the intrinsic disorder content is highly variable in viral genomes. Over the years, functional annotations of disordered regions at the scale of the whole proteome have been conducted for several animal viruses. But to date, similar studies applied to plant viruses are still missing. Based on disorder prediction tools combined with annotation programs and evolutionary studies, we analyzed the intrinsic disorder content in Potyvirus, using a 10-species dataset representative of this genus diversity. In this paper, we revealed that: (i) the Potyvirus proteome displays high disorder content, (ii) disorder is conserved during Potyvirus evolution, suggesting a functional advantage of IDRs, (iii) IDRs evolve faster than ordered regions, and (iv) IDRs may be associated with major biological functions required for the Potyvirus cycle. Notably, the proteins P1, Coat protein (CP) and Viral genome-linked protein (VPg) display a high content of conserved disorder, enriched in specific motifs mimicking eukaryotic functional modules and suggesting strategies of host machinery hijacking. In these three proteins, IDRs are particularly conserved despite their high amino acid polymorphism, indicating a link to adaptive processes. Through this comprehensive study, we further investigate the biological relevance of intrinsic disorder in Potyvirus biology and we propose a functional annotation of potyviral proteome IDRs.