Kitagaki H, Shimoi H, Itoh K
National Research Institute of Brewing, Higashihiroshima, Japan.
Eur J Biochem. 1997 Oct 1;249(1):343-9. doi: 10.1111/j.1432-1033.1997.t01-1-00343.x.
A 100-kDa protein was found to be a major cell wall protein in Saccharomyces cerevisiae cells cultured without shaking, but was not present in cells cultured with shaking. The amino acid sequence of this protein was identical to the sequence of Tir1p/Srp1p. TIR1/SRP1 has previously been identified as a gene induced by glucose, cold shock or anaerobiosis and was believed to be a cell membrane protein but not a cell wall protein. However, we found that beta-1,3-glucanase solubilized Tir1p/Srp1p from the cell wall and the purified Tir1p/Srp1p reacted with antiserum to beta-1,6-glucan and contained glucose. These results suggest that Tir1p/Srp1p is a major structural cell wall protein in the static-cultured yeast cells and is bound to the cell wall through beta-1,6-glucan. TIR1/SRP1 mRNA was transcribed only in the static culture and its transcription was regulated by the ROX1 repressor.
在未摇床培养的酿酒酵母细胞中，一种100 kDa的蛋白质被发现是主要的细胞壁蛋白，但在摇床培养的细胞中不存在。该蛋白质的氨基酸序列与Tir1p/Srp1p的序列相同。TIR1/SRP1先前已被鉴定为受葡萄糖、冷休克或厌氧诱导的基因，并且被认为是一种细胞膜蛋白而非细胞壁蛋白。然而，我们发现β-1,3-葡聚糖酶可从细胞壁中溶解Tir1p/Srp1p，并且纯化的Tir1p/Srp1p与抗β-1,6-葡聚糖抗血清反应并含有葡萄糖。这些结果表明，Tir1p/Srp1p是静态培养酵母细胞中的主要结构性细胞壁蛋白，并通过β-1,6-葡聚糖与细胞壁结合。TIR1/SRP1 mRNA仅在静态培养中转录，其转录受ROX1阻遏物调控。
