Cloning and characterization of decaprenyl diphosphate synthase from three different fungi

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• 作者：Daisuke Moriyama ; Tomohiro Kaino…
• 关键词：Coenzyme Q ; CoQ ; Ubiquinone ; Decaprenyl diphosphate synthase ; Fission yeast
• 刊名：Applied Microbiology and Biotechnology
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：101
• 期：4
• 页码：1559-1571
• 全文大小：
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Microbiology; Microbial Genetics and Genomics; Biotechnology;
• 出版者：Springer Berlin Heidelberg
• ISSN：1432-0614
• 卷排序：101

文摘

Coenzyme Q (CoQ) is composed of a benzoquinone moiety and an isoprenoid side chain of varying lengths. The length of the side chain is controlled by polyprenyl diphosphate synthase. In this study, dps1 genes encoding decaprenyl diphosphate synthase were cloned from three fungi: Bulleromyces albus, Saitoella complicata, and Rhodotorula minuta. The predicted Dps1 proteins contained seven conserved domains found in typical polyprenyl diphosphate synthases and were 528, 440, and 537 amino acids in length in B. albus, S. complicata, and R. minuta, respectively. Escherichia coli expressing the fungal dps1 genes produced CoQ₁₀ in addition to endogenous CoQ₈. Two of the three fungal dps1 genes (from S. complicata and R. minuta) were able to replace the function of ispB in an E. coli mutant strain. In vitro enzymatic activities were also detected in recombinant strains. The three dps1 genes were able to complement a Schizosaccharomyces pombedps1, dlp1 double mutant. Recombinant S. pombe produced mainly CoQ₁₀, indicating that the introduced genes were independently functional and did not require dlp1. The cloning of dps1 genes from various fungi has the potential to enhance production of CoQ₁₀ in other organisms.