二酰基甘油激酶蛋白家族的系统发育分析以及在催化域内多个高度特异性的保守插入和缺失的鉴定，这是不同类别的DGK同源物的独特特征。,PLOS ONE

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二酰基甘油激酶蛋白家族的系统发育分析以及在催化域内多个高度特异性的保守插入和缺失的鉴定，这是不同类别的DGK同源物的独特特征。
PLOS ONE ( IF 2.9 ) Pub Date : 2017-08-23 , DOI: 10.1371/journal.pone.0182758
Radhey S Gupta ₁ , Richard M Epand ₁

Affiliation

将二酰基甘油磷酸化为磷脂酸的二酰基甘油激酶（DGK）蛋白质家族在控制真核生物的多种细胞过程中起着重要作用。大多数脊椎动物物种包含10种不同的DGK同工酶，根据特定功能域的存在与否，它们分为5种不同的类别。但是，尚不清楚不同DGK同工酶之间的关系或它们如何从共同祖先进化而来。催化结构域构成了DGK蛋白中单个最大的序列元素，所有家族成员普遍且唯一地共享该催化元素，但是对该结构域的整体功能了解有限。在这项工作中，我们已经使用催化结构域序列为主要脊椎动物类的代表的DGK家族成员构建了系统树，并且还研究了真核生物门中各种DGK同工酶的分布。在基于催化结构域序列的树中，属于不同类别的DGK同源物形成了强支撑的簇，这些簇被长分支隔开，并且每个类别中的不同同工酶通常也形成了单系统分类。此外，我们对催化结构域序列比对的分析已鉴定出> 10个由保守签名插入片段（插入或缺失，CSI）组成的10个新序列签名，它们是DGK同工酶的特定类型的独特特征，或通常由两个成员共享或更多类DGK同工酶。已知蛋白质序列中的保守插入缺失在发现它们的蛋白质/生物中起重要的功能作用。因此，我们鉴定出多个不同类别的DGK同源物的特征的多个高度特异的CSI，表明DGK同工酶在催化结构域功能上存在重要差异。鉴定出的CSI与爆炸搜索DGK同工酶物种分布的结果相结合，也为了解DGK蛋白质家族之间的进化关系提供了有用的见识。我们鉴定出具有不同类别DGK同源物特征的多个高特异性CSI，这表明DGK同工酶在催化域功能上存在重要差异。鉴定出的CSI与爆炸搜索DGK同工酶物种分布的结果相结合，也为了解DGK蛋白质家族之间的进化关系提供了有用的见识。我们鉴定出具有不同类别DGK同源物特征的多个高特异性CSI，这表明DGK同工酶在催化域功能上存在重要差异。鉴定出的CSI与爆炸搜索DGK同工酶物种分布的结果相结合，也为了解DGK蛋白质家族之间的进化关系提供了有用的见识。

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Phylogenetic analysis of the diacylglycerol kinase family of proteins and identification of multiple highly-specific conserved inserts and deletions within the catalytic domain that are distinctive characteristics of different classes of DGK homologs.

Diacylglycerol kinase (DGK) family of proteins, which phosphorylates diacylglycerol into phosphatidic acid, play important role in controlling diverse cellular processes in eukaryotic organisms. Most vertebrate species contain 10 different DGK isozymes, which are grouped into 5 different classes based on the presence or absence of specific functional domains. However, the relationships among different DGK isozymes or how they have evolved from a common ancestor is unclear. The catalytic domain constitutes the single largest sequence element within the DGK proteins that is commonly and uniquely shared by all family members, but there is limited understanding of the overall function of this domain. In this work, we have used the catalytic domain sequences to construct a phylogenetic tree for the DGK family members from representatives of the main vertebrate classes and have also examined the distributions of various DGK isozymes in eukaryotic phyla. In a tree based on catalytic domain sequences, the DGK homologs belonging to different classes formed strongly supported clusters which were separated by long branches, and the different isozymes within each class also generally formed monophyletic groupings. Further, our analysis of the sequence alignments of catalytic domains has identified >10 novel sequence signatures consisting of conserved signature indels (inserts or deletions, CSIs) that are distinctive characteristics of either particular classes of DGK isozymes, or are commonly shared by members of two or more classes of DGK isozymes. The conserved indels in protein sequences are known to play important functional roles in the proteins/organisms where they are found. Thus, our identification of multiple highly specific CSIs that are distinguishing characteristics of different classes of DGK homologs points to the existence of important differences in the catalytic domain function among the DGK isozymes. The identified CSIs in conjunction with the results of blast searches on species distribution of DGK isozymes also provide useful insights into the evolutionary relationships among the DGK family of proteins.

更新日期：2019-11-01

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