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首页> 外文期刊>Applied Microbiology >Use of the Yeast Pichia pastoris as an Expression Host for Secretion of Enterocin L50, a Leaderless Two-Peptide (L50A and L50B) Bacteriocin from Enterococcus faecium L50
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Use of the Yeast Pichia pastoris as an Expression Host for Secretion of Enterocin L50, a Leaderless Two-Peptide (L50A and L50B) Bacteriocin from Enterococcus faecium L50

机译：酵母毕赤酵母作为表达宿主分泌屎肠球菌L50肠球菌L50（无领导型两肽（L50A和L50B）细菌素）的表达宿主的用途

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摘要

In this work, we report the expression and secretion of the leaderless two-peptide (EntL50A and EntL50B) bacteriocin enterocin L50 from Enterococcus faecium L50 by the methylotrophic yeast Pichia pastoris X-33. The bacteriocin structural genes entL50A and entL50B were fused to the Saccharomyces cerevisiae gene region encoding the mating pheromone α-factor 1 secretion signal ( MF α 1_(s) ) and cloned, separately and together ( entL50AB ), into the P. pastoris expression and secretion vector pPICZαA, which contains the methanol-inducible alcohol oxidase promoter (P_(AOX1)) to express the fusion genes. After transfer into the yeast, the recombinant plasmids were integrated into the genome, resulting in three bacteriocinogenic yeast strains able to produce and secrete the individual bacteriocin peptides EntL50A and EntL50B separately and together. The secretion was efficiently directed by MFα1_(s) through the Sec system, and the precursor peptides were found to be correctly processed to form mature and active bacteriocin peptides. The present work describes for the first time the heterologous expression and secretion of a two-peptide non-pediocin-like bacteriocin by a yeast.
机译：在这项工作中，我们报告了甲基营养酵母巴斯德毕赤酵母X-33从粪肠球菌L50表达和分泌无前导性两肽（EntL50A和EntL50B）细菌素肠球蛋白L50。将细菌素结构基因entL50A和entL50B与编码交配信息素α-因子1分泌信号（MFα1_（s））的酿酒酵母基因区融合，并分别和一起（entL50AB）克隆到巴斯德毕赤酵母的表达和分泌载体pPICZαA，其中包含甲醇诱导型醇氧化酶启动子（P_（AOX1））以表达融合基因。转移到酵母中后，将重组质粒整合到基因组中，从而产生三种能够分别产生并分泌出单独的细菌素肽EntL50A和EntL50B的致细菌性酵母菌株。 MFα1_（s）通过Sec系统有效地指导了分泌，并且发现前体肽被正确加工形成成熟的活性细菌素肽。本工作首次描述了酵母中两肽非花椒素样细菌素的异源表达和分泌。

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