Comparative genomic study of protein disulfide isomerases from photosynthetic organisms
Comparative genomic study of protein disulfide isomerases from photosynthetic organisms
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DOI：
10.1016/j.ygeno.2010.10.001
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发表时间：
2011-01-01
期刊：
影响因子：
4.4
通讯作者：
Rouhier, Nicolas
中科院分区：
文献类型：
--
作者：
Selles, Benjamin;Jacquot, Jean-Pierre;Rouhier, Nicolas
蛋白质二硫键异构酶（PDI）是真核生物蛋白质氧化折叠所必需的氧化还原酶。通过分析藻类、石松、苔藓和被子植物门的24个已测序基因组，评估了它们在光合生物中的多样性。该系统发育分析导致更新的分类为9类（PDI-A至-F、-L、-M和-S），其不同之处在于Trx结构域的数量和其他结构域（D、COPII、J和ARMET）的存在。从进化的角度来看，PDI的分布和蛋白质结构在藻类和陆生植物之间有很大的不同，5个PDI类是常见的，而1个是陆生植物特有的，3个是藻类特有的。一些藻类PDI-F具有硒代半胱氨酸残基。PDI家族在哺乳动物（人类19个成员）中比在陆地植物（约10个成员）和酿酒酵母（5个成员）中更大。然而，光合生物的PDIs显示出重要的结构和功能多样性，考虑到它们与特定蛋白质结构域的关联。(C)2010年爱思唯尔公司All rights reserved.
Protein disulfide isomerases (PDIs) are eukaryotic oxidoreductases essential for oxidative protein folding. Their diversity in photosynthetic organisms was assessed by analyzing 24 sequenced genomes belonging to algal, lycophyte, bryophyte and angiosperm phyla. This phylogenetic analysis led to an updated classification into 9 classes (PDI-A to -F, -L, -M and -S) which differed by the number of Trx domains and the presence of additional domains (D, COPII, J and ARMET). From an evolutionary perspective, the distribution and protein architecture of PDIs differ considerably between algae and terrestrial plants, 5 PDI classes are common whereas 1 is specific to terrestrial plants and 3 to algae. Some algal PDI-Fs possess selenocysteine residues. The PDI family is larger in mammals (19 members in human) than in land plants (around 10 members) and Saccharomyces cerevisiae (5 members). However, PDIs from photosynthetic organisms display an important structural and functional diversity considering their association to specific protein domains. (C) 2010 Elsevier Inc. All rights reserved.