Drug Discoveries & Therapeutics
Online ISSN : 1881-784X
Print ISSN : 1881-7831
ISSN-L : 1881-7831
Original Articles
Cloning and expression analysis of squalene synthase, a key enzyme involved in antifungal steroidal glycoalkaloids biosynthesis from Solanum nigrum
Yi SunYing ZhaoLei WangHongxiang LouAixia Cheng
Author information
JOURNALS FREE ACCESS

2012 Volume 6 Issue 5 Pages 242-248

Details
Abstract

Steroidal glycoalkaloids (SGAs) are a family of nitrogenous secondary metabolites produced in solanaceous plants. In our present study, γ-solamargine and its aglycone solasodine from Solanum nigrum were found to inhibit hyphae formation of Fusarium oxysporum. As phytoalexins, the formation of SGAs was significantly increased in the plants when infected with the spore of F. oxysporum. In order to understand this inducible defense mechanism, the rate-limiting enzyme squalene synthase in the biosynthesis process of SGAs was investigated well. A full-length cDNA encoding squalene synthase was isolated from S. nigrum (the squalene synthase in S. nigrum was designated as SnSS). The full-length cDNA of SnSS was 1,765 bp and contained a 1,236 bp open reading frame (ORF) encoding a polypeptide of 411 amino acids. Bioinformatic analysis revealed that the deduced SnSS protein had a high similarity with other plant squalene synthases. Real-time RT-PCR analysis showed that SnSS was expressed constitutively in all tested tissues, with the highest expression in stems. After treatment with the spore of F. oxysporum, the mRNA level of SnSS was significantly increased in the infected plants in accordance with the change of SGAs.

Information related to the author
© 2012 International Research and Cooperation Association for Bio & Socio-Sciences Advancement
Previous article Next article
feedback
Top