Evolution of the KCS gene family in plants: the history of gene duplication, sub/neofunctionalization and redundancy
Evolution of the KCS gene family in plants: the history of gene duplication, sub/neofunctionalization and redundancy
复制标题
植物中 KCS 基因家族的进化:基因复制、亚/新功能化和冗余的历史
DOI:
10.1007/s00438-015-1142-3
复制
发表时间:
2016-04-01
影响因子:
3.1
通讯作者:
Xue, Jia-Yu
中科院分区:
文献类型:
--
作者:
Guo, Hai-Song;Zhang, Yan-Mei;Xue, Jia-Yu
Very long-chain fatty acids (VLCFAs) play an important role in the survival and development of plants, and VLCFA synthesis is regulated by beta-ketoacyl-CoA synthases (KCSs), which catalyze the condensation of an acyl-CoA with malonyl-CoA. Here, we present a genome-wide survey of the genes encoding these enzymes, KCS genes, in 28 species (26 genomes and two transcriptomes), which represents a large phylogenetic scale, and also reconstruct the evolutionary history of this gene family. KCS genes were initially single-copy genes in the green plant lineage; duplication resulted in five ancestral copies in land plants, forming five fundamental monophyletic groups in the phylogenetic tree. Subsequently, KCS genes duplicated to generate 11 genes of angiosperm origin, expanding up to 20-30 members in further-diverged angiosperm species. During this process, tandem duplications had only a small contribution, whereas polyploidy events and large-scale segmental duplications appear to be the main driving force. Accompanying this expansion were variations that led to the sub- and neofunctionalization of different members, resulting in specificity that is likely determined by the 3-D protein structure. Novel functions involved in other physiological processes emerged as well, though redundancy is also observed, largely among recent duplications. Conserved sites and variable sites of KCS proteins are also identified by statistical analysis. The variable sites are likely to be involved in the emergence of product specificity and catalytic power, and conserved sites are possibly responsible for the preservation of fundamental function.