Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina út 29, H-1113 Budapest, Hungary.
Infect Genet Evol. 2011 Jul;11(5):1037-44. doi: 10.1016/j.meegid.2011.03.023. Epub 2011 Apr 2.
A new protein, termed apicortin, has recently been identified, which occurs only in the placozoan animal Trichoplax adhaerens and in the genomes of all currently sequenced apicomplexan parasites (e.g., Toxoplasma, Plasmodium, etc.). Apicortins unite two conserved domains, a DCX motif and a partial p25alpha sequence, which are singly found in diverse other proteins, in doublecortins and TPPPs, respectively. Here I show that although apicortin has a limited phylogenomic distribution, its occurrence is broader than thought previously. It has been identified in another primitive opisthokont, in the chytrid fungus, Spizellomyces punctatus. Apicortins can be divided into two subgroups: apicomplexan and non-apicomplexan ones. The main difference is that the former ones possess a long, N-terminal extension predicted to be disordered, which is missing in the other subgroup. The appearance of the extension in apicomplexan apicortins is an "innovation" of this phylum, and may play a functional role in the protein-protein interactions.
最近发现了一种新的蛋白质,称为质膜联蛋白(apicortin),它仅存在于扁盘动物 Trichoplax adhaerens 以及所有目前测序的顶复门寄生虫(如弓形虫、疟原虫等)的基因组中。质膜联蛋白将两个保守结构域,即 DCX 基序和 p25alpha 序列的一部分,分别结合在一起,这两个结构域在其他多种蛋白质中单独存在,分别为双皮质素和 TPPP。在这里,我表明尽管质膜联蛋白的系统发生分布有限,但它的出现比以前认为的更为广泛。它已在另一种原始后口动物、粘菌 Spizellomyces punctatus 中被发现。质膜联蛋白可以分为两个亚组:顶复门亚组和非顶复门亚组。主要区别在于前者具有一个预测为无序的长 N 端延伸,而后者则没有。在顶复门质膜联蛋白中,延伸的出现是这个门的一个“创新”,可能在蛋白质-蛋白质相互作用中发挥功能作用。