A Hyperthermophilic Phage Decoration Protein Suggests Common Evolutionary Origin with Herpesvirus Triplex Proteins and an Anti-CRISPR Protein.
A Hyperthermophilic Phage Decoration Protein Suggests Common Evolutionary Origin with Herpesvirus Triplex Proteins and an Anti-CRISPR Protein.
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超嗜热噬菌体装饰蛋白表明与疱疹病毒三链体蛋白和抗 CRISPR 蛋白具有共同的进化起源。
DOI：
10.1016/j.str.2018.04.008
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发表时间：
2018
期刊：
影响因子：
--
通讯作者：
Kelch,BrianA
中科院分区：
文献类型：
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作者：
Stone,NicholasP;Hilbert,BrendanJ;Hidalgo,Daniel;Halloran,KevinT;Lee,Jooyoung;Sontheimer,ErikJ;Kelch,BrianA
病毒衣壳是保护病毒基因组免受环境攻击的蛋白质外壳，同时保持紧密包装的基因组的高内部压力。为了阐明衣壳如何在恶劣条件下保持稳定性，我们研究了超嗜热噬菌体P74-26的衣壳成分。我们确定了衣壳蛋白gp87的结构，并表明它与许多其他噬菌体中的装饰蛋白具有相同的折叠，尽管缺乏显著的序列同源性。我们还发现gp87明显比中温同源物更稳定。我们对gp87结构的分析表明，核心“β郁金香”结构域在许多双链DNA病毒（包括疱疹病毒）的三聚体衣壳成分中是保守的。此外，在抗crispr蛋白AcrIIC1中发现了β桶结构域，这提示了这种Cas9抑制剂的进化机制。我们的工作阐明了gp87稳定性增加的原理，并扩展了β郁金香结构域的进化范围。
Virus capsids are protein shells that protect the viral genome from environmental assaults, while maintaining the high internal pressure of the tightly packaged genome. To elucidate how capsids maintain stability under harsh conditions, we investigated the capsid components of the hyperthermophilic phage P74-26. We determined the structure of capsid protein gp87 and show that it has the same fold as decoration proteins in many other phages, despite lacking significant sequence homology. We also find that gp87 is significantly more stable than mesophilic homologs. Our analysis of the gp87 structure reveals that the core "β tulip" domain is conserved in trimeric capsid components across numerous double-stranded DNA viruses, including Herpesviruses. Moreover, this β barrel domain is found in anti-CRISPR protein AcrIIC1, suggesting a mechanism for the evolution of this Cas9 inhibitor. Our work illustrates the principles for increased stability of gp87, and extends the evolutionary reach of the β tulip domain.