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Cloning and characterization of squalene synthase gene from Fusarium fujikuroi (Saw.) Wr.
Zhao, Rui-Yu; Xiao, Wei; Cheng, Hai-Li; Zhu, Ping; Cheng, Ke-Di.
Afiliação
  • Zhao RY; Department of Biosynthesis of Natural Products, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, 1 Xian Nong Tan Street, Beijing, 100050, China.
J Ind Microbiol Biotechnol ; 37(11): 1171-82, 2010 Nov.
Article em En | MEDLINE | ID: mdl-20585832
The gene encoding squalene synthase (GfSQS) was cloned from Fusarium fujikuroi (Gibberella fujikuroi MP-C) and characterized. The cloned genomic DNA is 3,267 bp in length, including the 5'-untranslated region (UTR), 3'-UTR, four exons, and three introns. A noncanonical splice-site (CA-GG, or GC-AG) was found at the first intron. The open reading frame of the gene is 1,389 bp in length, corresponding to a predicted polypeptide of 462 amino acid residues with a MW 53.4 kDa. The predicted GfSQS shares at least four conserved regions involved in the enzymatic activity with the SQSs of varied species. The recombinant protein was expressed in E. coli and detected by SDS-PAGE and western blot. GC-MS analysis showed that the wild-type GfSQS could catalyze the reaction from farnesyl diphosphate (FPP) to squalene, while the mutant mGfSQS (D82G) lost total activity, supporting the prediction that the aspartate-rich motif (DTXED) in the region I of SQS is essential for binding of the diphosphate substrate.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Farnesil-Difosfato Farnesiltransferase / Proteínas Fúngicas / Fusarium Idioma: En Ano de publicação: 2010 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Farnesil-Difosfato Farnesiltransferase / Proteínas Fúngicas / Fusarium Idioma: En Ano de publicação: 2010 Tipo de documento: Article