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Molecular characterization and functional analysis of chalcone synthase from Syringa oblata Lindl. in the flavonoid biosynthetic pathway.
Wang, Yu; Dou, Ying; Wang, Rui; Guan, Xuelian; Hu, Zenghui; Zheng, Jian.
Afiliación
  • Wang Y; College of Landscape Architecture, Beijing University of Agriculture, Beijing 102206, China.
  • Dou Y; College of Landscape Architecture, Beijing University of Agriculture, Beijing 102206, China.
  • Wang R; College of Landscape Architecture, Beijing University of Agriculture, Beijing 102206, China.
  • Guan X; College of Landscape Architecture, Beijing University of Agriculture, Beijing 102206, China.
  • Hu Z; College of Landscape Architecture, Beijing University of Agriculture, Beijing 102206, China; Beijing Collaborative Innovation Center for Eco-Environmental Improvement with Forestry and Fruit Trees, Beijing 102206, China.
  • Zheng J; College of Landscape Architecture, Beijing University of Agriculture, Beijing 102206, China; Beijing Collaborative Innovation Center for Eco-Environmental Improvement with Forestry and Fruit Trees, Beijing 102206, China. Electronic address: zhengjian@bac.edu.cn.
Gene ; 635: 16-23, 2017 Nov 30.
Article en En | MEDLINE | ID: mdl-28890377
The flower color of Syringa oblata Lindl., which is often modulated by the flavonoid content, varies and is an important ornamental feature. Chalcone synthase (CHS) catalyzes the first key step in the flavonoid biosynthetic pathway. However, little is known about the role of S. oblata CHS (SoCHS) in flavonoid biosynthesis in this species. Here, we isolate and analyze the cDNA (SoCHS1) that encodes CHS in S. oblata. We also sought to analyzed the molecular characteristics and function of flavonoid metabolism by SoCHS1. We successfully isolated the CHS-encoding genomic DNA (gDNA) in S. oblata (SoCHS1), and the gene structural analysis indicated it had no intron. The opening reading frame (ORF) sequence of SoCHS1 was 1170bp long and encoded a 389-amino acid polypeptide. Multiple sequence alignment revealed that both the conserved CHS active site residues and CHS signature sequence were in the deduced amino acid sequence of SoCHS1. Crystallographic analysis revealed that the protein structure of SoCHS1 is highly similar to that of FnCHS1 in Freesia hybrida. The quantitative real-time polymerase chain reaction (PCR) performed to detect the SoCHS1 transcript expression levels in flowers, and other tissues revealed the expression was significantly correlated with anthocyanin accumulation during flower development. The ectopic expression results of Nicotiana tabacum showed that SoCHS1 overexpression in transgenic tobacco changed the flower color from pale pink to pink. In conclusion, these results suggest that SoCHS1 plays an essential role in flavonoid biosynthesis in S. oblata, and could be used to modify flavonoid components in other plant species.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Flavonoides / Aciltransferasas / Flores / Vías Biosintéticas Idioma: En Revista: Gene Año: 2017 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Flavonoides / Aciltransferasas / Flores / Vías Biosintéticas Idioma: En Revista: Gene Año: 2017 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos