BBX proteins in green plants: Insights into their evolution, structure, feature and functional diversification
BBX proteins in green plants: Insights into their evolution, structure, feature and functional diversification
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DOI：
10.1016/j.gene.2013.08.037
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发表时间：
2013-11-15
期刊：
影响因子：
3.5
通讯作者：
Botto, Javier F.
中科院分区：
文献类型：
--
作者：
Crocco, Carlos D.;Botto, Javier F.
B - box结构域在动植物物种中大量参与细胞生长控制、分化和转录调控的蛋白质中是保守的。在拟南芥中，一些研究发现B - box蛋白（BBX）在开花、光和非生物胁迫信号传导中发挥着核心的发育功能。尽管这个蛋白家族在功能上很重要，但在植物界中，BBX蛋白的进化和结构关系尚未得到广泛研究。利用系统发育方法，我们对12种植物（4种绿藻、1种苔藓、1种石松类植物、3种单子叶植物和3种双子叶植物）中的BBX蛋白家族进行了全面的进化分析。分析将214个BBX蛋白分为5个结构组，它们在绿色植物进化的早期阶段独立进化。我们表明每个结构组的B - box共有序列保留了一种共同且保守的结构域拓扑结构。此外，我们确定了每个结构组特有的7个新基序以及在一些BBX蛋白的C末端结构域中保守的缬氨酸 - 脯氨酸（VP）对，这表明它们是蛋白质 - 蛋白质相互作用所必需的。正如在哺乳动物系统中所记载的那样，我们还在C末端结构域发现了可作为核定位信号（NLSs）的单部分和双部分氨基酸序列。5个BBX结构组的进化受到两个B - box中氨基酸序列保守性的限制，但在每个结构组的NLSs和新基序上产生了辐射状变异。我们认为这些特征是绿色植物中BBX蛋白多样性的功能基础。（C）2013爱思唯尔公司。保留所有权利。
The B-box domain is conserved in a large number of proteins involved in cell growth control, differentiation and transcriptional regulation among animal and plant species. In Arabidopsis thaliana, some works have found that B-box proteins (BOX) play central developmental functions in flowering, light and abiotic stress signaling. Despite the functional importance of this protein family, evolutionary and structural relationships of BBX proteins have not been extensively investigated in the plant kingdom. Using a phylogenetic approach, we conducted a comprehensive evolutionary analysis of the BBX protein family in twelve plant species (four green algae, one moss, one lycophyte, three monocots and three dicots). The analysis classified 214 BOX proteins into five structure groups, which evolved independently at early stages of green plant evolution. We showed that the B-box consensus sequences of each structure groups retained a common and conserved domain topology. Furthermore, we identified seven novel motifs specific to each structure group and a valine-proline (VP) pair conserved at the C-terminus domain in some BBX proteins suggesting that they are required for protein-protein interactions. As it has been documented in mammalian systems, we also found monopartite and bipartite amino acid sequences at the C-terminus domain that could function as nuclear localization signals (NLSs). The five BBX structure groups evolved constrained by the conservation of amino acid sequences in the two B-boxes, but radiating variation into NLSs and novel motifs of each structural group. We suggest that these features are the functional basis for the BBX protein diversity in green plants. (C) 2013 Elsevier B.V. All rights reserved.