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首页> 外文期刊>Journal of bacteriology >Sed1p Is a Major Cell Wall Protein ofSaccharomyces cerevisiae in the Stationary Phase and Is Involved in Lytic Enzyme Resistance
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Sed1p Is a Major Cell Wall Protein ofSaccharomyces cerevisiae in the Stationary Phase and Is Involved in Lytic Enzyme Resistance

机译：Sed1p是酿酒酵母在静止期的主要细胞壁蛋白，参与了溶菌酶的抗性

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A 260-kDa structural cell wall protein was purified from sodium dodecyl sulfate-treated cell walls of Saccharomyces cerevisiae by incubation with Rarobacter faecitabidusprotease I, which is a yeast-lytic enzyme. Amino acid sequence analysis revealed that this protein is the product of the SED1 gene.SED1 was formerly identified as a multicopy suppressor oferd2, which encodes a protein involved in retrieval of luminal endoplasmic reticulum proteins from the secretory pathway. Sed1p is very rich in threonine and serine and, like other structural cell wall proteins, contains a putative signal sequence for the addition of a glycosylphosphatidylinositol anchor. However, the fact that Sed1p, unlike other cell wall proteins, has six cysteines and seven putative N-glycosylation sites suggests that Sed1p belongs to a new family of cell wall proteins. Epitope-tagged Sed1p was detected in a β-1,3-glucanase extract of cell walls by immunoblot analysis, suggesting that Sed1p is a glucanase-extractable cell wall protein. The expression of Sed1p mRNA increased in the stationary phase and was accompanied by an increase in the Sed1p content of cell walls. Disruption of SED1 had no effect on exponentially growing cells but made stationary-phase cells sensitive to Zymolyase. These results indicate that Sed1p is a major structural cell wall protein in stationary-phase cells and is required for lytic enzyme resistance.
机译：通过用酵母水解酶 Rarobacter faecitabidus 蛋白酶I孵育，从十二烷基硫酸钠处理过的酿酒酵母的细胞壁中纯化出一个260 kDa的结构细胞壁蛋白。 。氨基酸序列分析表明该蛋白是 SED1 基因的产物。 SED1 以前被鉴定为 erd2 的多拷贝抑制剂，其编码一种从分泌途径中获取管腔内质网蛋白的蛋白。 Sed1p非常富含苏氨酸和丝氨酸，并且像其他结构性细胞壁蛋白一样，包含一个假定的信号序列，用于添加糖基磷脂酰肌醇锚。但是，与其他细胞壁蛋白不同，Sed1p具有六个半胱氨酸和七个推定的N-糖基化位点这一事实表明Sed1p属于细胞壁蛋白的新家族。通过免疫印迹分析在细胞壁的β-1,3-葡聚糖酶提取物中检测到带有抗原表位的Sed1p，这表明Sed1p是可从葡聚糖酶提取的细胞壁蛋白。 Sed1p mRNA的表达在固定相中增加，并伴随着细胞壁中Sed1p含量的增加。 SED1 的破坏对指数生长的细胞没有影响，但使固定相细胞对酶合酶敏感。这些结果表明，Sed1p是固定相细胞中的主要结构细胞壁蛋白，是耐裂解酶的必需蛋白。

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