Department of Functional and Evolutionary Ecology, University of Vienna, Djerassiplatz 1, 1030 Wien, Austria.
Department of Functional and Evolutionary Ecology, University of Vienna, Djerassiplatz 1, 1030 Wien, Austria.
Biochim Biophys Acta Bioenerg. 2023 Jan 1;1864(1):148916. doi: 10.1016/j.bbabio.2022.148916. Epub 2022 Sep 6.
Succinate dehydrogenases (SDHs) and fumarate reductases (FRDs) catalyse the interconversion of succinate and fumarate, a reaction highly conserved in all domains of life. The current classification of SDH/FRDs is based on the structure of the membrane anchor subunits and their cofactors. It is, however, unknown whether this classification would hold in the context of evolution. In this work, a large-scale comparative genomic analysis of complex II addresses the questions of its taxonomic distribution and phylogeny. Our findings report that for types C, D, and F, structural classification and phylogeny go hand in hand, while for types A, B and E the situation is more complex, highlighting the possibility for their classification into subgroups. Based on these findings, we proposed a revised version of the evolutionary scenario for these enzymes in which a primordial soluble module, corresponding to the cytoplasmatic subunits, would give rise to the current diversity via several independent membrane anchor attachment events.
琥珀酸脱氢酶（SDH）和延胡索酸还原酶（FRD）催化琥珀酸和富马酸的相互转化，这是所有生命领域中高度保守的反应。SDH/FRD 的现行分类是基于膜锚定亚基及其辅因子的结构。然而，在进化的背景下，这种分类是否成立尚不清楚。在这项工作中，对复合物 II 进行了大规模的比较基因组分析，以解决其分类分布和系统发育的问题。我们的研究结果表明，对于类型 C、D 和 F，结构分类和系统发育是一致的，而对于类型 A、B 和 E，情况则更为复杂，这突出了它们分类为亚组的可能性。基于这些发现，我们提出了这些酶的进化情景的修订版本，其中原始的可溶性模块，对应于细胞质亚基，将通过几个独立的膜锚定附着事件产生当前的多样性。
