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Global analysis of non-animal peroxidases provides insights into the evolution of this gene family in the green lineage.
Journal of Experimental Botany ( IF 6.9 ) Pub Date : 2020-03-18 , DOI: 10.1093/jxb/eraa141
Duchesse Lacour Mbadinga Mbadinga 1 , Qiang Li 1, 2 , Philippe Ranocha 1 , Yves Martinez 3 , Christophe Dunand 1
Affiliation  

The non-animal peroxidases belong to a superfamily of oxidoreductases that reduce hydrogen peroxide and oxidize numerous substrates. Since their initial characterization in 1992, a number of studies have provided an understanding of the origin and evolution of this protein family. Here, we report a comprehensive evolutionary analysis of non-animal peroxidases using integrated in silico and biochemical approaches. Thanks to the availability of numerous genomic sequences from more than 2500 species belonging to 14 kingdoms together with expert and comprehensive annotation of peroxidase sequences that have been centralized in a dedicated database, we have been able to use phylogenetic reconstructions to increase our understanding of the evolutionary processes underlying the diversification of non-animal peroxidases. We analysed the distribution of all non-animal peroxidases in more than 200 eukaryotic organisms in silico. First, we show that the presence or absence of non-animal peroxidases correlates with the presence or absence of certain organelles or with specific biological processes. Examination of almost 2000 organisms determined that ascorbate peroxidases (APxs) and cytochrome c peroxidases (CcPs) are present in those containing chloroplasts and mitochondria, respectively. Plants, which contain both organelles, are an exception and contain only APxs without CcP. Class II peroxidases (CII Prxs) are only found in fungi with wood-decay and plant-degradation abilities. Class III peroxidases (CIII Prxs) are only found in streptophyte algae and land plants, and have been subjected to large family expansion. Biochemical activities of APx, CcP, and CIII Prx assessed using protein extracts from 30 different eukaryotic organisms support the distribution of the sequences resulting from our in silico analysis. The biochemical results confirmed both the presence and classification of the non-animal peroxidase encoding sequences.

中文翻译:

对非动物过氧化物酶的全局分析提供了对该谱系在绿色谱系中进化的见解。

非动物过氧化物酶属于氧化还原酶的超家族,其还原过氧化氢并氧化多种底物。自从1992年对其进行初步表征以来,许多研究提供了对该蛋白家族的起源和进化的理解。在这里,我们报告了使用集成计算机技术对非动物过氧化物酶的全面进化分析和生化方法。得益于来自14个王国的2500多个物种的众多基因组序列的可用性,以及过氧化物酶序列的专家和全面注释(已集中在一个专用数据库中),我们能够使用系统发育重建来增进对进化论的理解。非动物过氧化物酶多样化的基本过程。我们分析了计算机中200多个真核生物中所有非动物过氧化物酶的分布。首先,我们表明非动物过氧化物酶的存在与否与某些细胞器的存在与否或特定的生物学过程有关。对近2000种生物的检查确定了抗坏血酸过氧化物酶(APxs)和细胞色素c过氧化物酶(CcPs)分别存在于含有叶绿体和线粒体的过氧化物酶中。包含两个细胞器的植物是一个例外,仅包含不含CcP的APx。II类过氧化物酶(CII Prxs)仅在具有木材腐烂和植物降解能力的真菌中发现。III类过氧化物酶(CIII Prxs)仅在链霉菌藻类和陆地植物中发现,并且已经经历了大家族扩张。使用来自30种不同的真核生物的蛋白质提取物评估的APx,CcP和CIII Prx的生化活性,支持了计算机分析的序列分布。生化结果证实了非动物过氧化物酶编码序列的存在和分类。
更新日期:2020-03-18
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