Zárate V, Belda F
Departamento de Microbiología y Biología Celular, Facultad de Farmacia, Universidad de La Laguna, Tenerife, Spain.
J Biotechnol. 1997 Apr 25;54(2):121-9. doi: 10.1016/s0168-1656(97)00042-4.
In order to gain information about the potential interest of the Schizosaccharomyces pombe srb 1 fragile mutants as a host for heterologous protein production, the extracellular secretion of homologous and heterologous invertases was investigated. Under catabolic derepression the fragile srb 1 mutants released into the extracellular medium 5-6-fold more invertase than the parental strain. When transformed with the SUC2 gene, which codes for Saccharomyces cerevisiae invertase, the srb 1-3 fragile mutant, grown under catabolic repression, released into the medium 3-fold more invertase than the wild-type transformant, even though the majority of the enzyme remained associated with the cell wall. Electrophoretic analysis revealed the presence in the fragile strains of some invertase forms with molecular weights smaller than their parallel wild-type strains, suggesting that the srb 1 mutants may underglycosylate not only their homologous but also the heterologous proteins.
为了获取粟酒裂殖酵母srb 1脆性突变体作为异源蛋白生产宿主的潜在价值信息，研究了同源和异源转化酶的细胞外分泌情况。在分解代谢去阻遏条件下，脆性srb 1突变体分泌到细胞外培养基中的转化酶比亲本菌株多5至6倍。当用编码酿酒酵母转化酶的SUC2基因转化时，在分解代谢阻遏条件下生长的srb 1-3脆性突变体分泌到培养基中的转化酶比野生型转化体多3倍，尽管大多数酶仍与细胞壁结合。电泳分析表明，脆性菌株中存在一些分子量比其平行野生型菌株小的转化酶形式，这表明srb 1突变体不仅可能对其同源蛋白，而且对异源蛋白进行低糖基化。
