Positive selection drives neofunctionalization of the UbiA prenyltransferase gene family
- 566 Downloads
Gene duplication provides the key materials for new genes and novel functions. However, the mechanism underlying functional innovation remains unknown. In this study, we revealed the evolutionary pattern of the prenyltransferases of the UbiA gene family in 15 higher plants. Prenyltransferases of the UbiA gene family are involved in many important biological processes of both primary and secondary metabolism. Based on the phylogenetic relationships of the UbiA genes, seven subfamilies are classified. Confirming this classification, genes within each subfamily are characterized by similar exon numbers, exon lengths and patterns of motif combinations. Similar numbers of UbiA genes are found in different species within each subfamily except for Subfamily I, in which a Phaseoleae-specific expansion is detected in clade I-A. Homologous genes in clade I-A evolve rapidly, exchange sequences frequently and experience positive selection. Genes in clade I-A function as flavonoid prenyltransferase synthesis secondary compounds, while other genes from Subfamily I encode homogentisate phytyltransferase, which plays a role in primary metabolism. Thus, our results suggest that the secondary metabolism genes acquire new functions from those of primary metabolism through gene duplication and neofunctionalization driven by positive selection.
KeywordsUbiA Prenyltransferase Evolution Gene duplication Positive selection Neofunctionalization
This work was supported in part by the National Natural Science Foundation of China (31301342, 31370034), Key Transgenic Breeding Program of China (2013ZX08004-003), Priority Academic Program Development of Jiangsu Higher Education Institutions Jiangsu Provincial Program (PAPD) and the Nanjing Agricultural University Youth Science and Technology Innovation Fund (KJ2013002).
- Akashi T, Sasaki K, Aoki T, Ayabe S, Yazaki K (2009) Molecular cloning and characterization of a cDNA for pterocarpan 4-dimethylallyltransferase catalyzing the key prenylation step in the biosynthesis of glyceollin, a soybean phytoalexin. Plant Physiol 149:683–693CrossRefPubMedCentralPubMedGoogle Scholar
- Hruz T, Laule O, Szabo G, Wessendorp F, Bleuler S, Oertle L, Widmayer P, Gruissem W, Zimmermann P (2008) Genevestigator v3: a reference expression database for the meta-analysis of transcriptomes. Adv Bioinform 2008:420747Google Scholar
- Okada K, Ohara K, Yazaki K, Nozaki K, Uchida N, Kawamukai M, Nojiri H, Yamane H (2004) The AtPPT1 gene encoding 4-hydroxybenzoate polyprenyl diphosphate transferase in ubiquinone biosynthesis is required for embryo development in Arabidopsis thaliana. Plant Mol Biol 55:567–577CrossRefPubMedGoogle Scholar
- Schmutz J, Cannon SB, Schlueter J, Ma J, Mitros T, Nelson W, Hyten DL, Song Q, Thelen JJ, Cheng J, Xu D, Hellsten U, May GD, Yu Y, Sakurai T, Umezawa T, Bhattacharyya MK, Sandhu D, Valliyodan B, Lindquist E, Peto M, Grant D, Shu S, Goodstein D, Barry K, Futrell-Griggs M, Abernathy B, Du J, Tian Z, Zhu L, Gill N, Joshi T, Libault M, Sethuraman A, Zhang XC, Shinozaki K, Nguyen HT, Wing RA, Cregan P, Specht J, Grimwood J, Rokhsar D, Stacey G, Shoemaker RC, Jackson SA (2010) Genome sequence of the palaeopolyploid soybean. Nature 463:178–183CrossRefPubMedGoogle Scholar
- Shimada H, Ohno R, Shibata M, Ikegami I, Onai K, Ohto MA, Takamiya K (2005) Inactivation and deficiency of core proteins of photosystems I and II caused by genetical phylloquinone and plastoquinone deficiency but retained lamellar structure in a T-DNA mutant of Arabidopsis. Plant J 41:627–637CrossRefPubMedGoogle Scholar