植物寄生真菌和贝克酵母的内质网亚室:管腔蛋白的差异分布

Ulrich Bachem, Kurt Mendgen
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引用次数: 9

摘要

Bachem, U, and Mendgen, K. 1995。植物寄生真菌和面包酵母的内质网亚室:管腔蛋白的差异分布。真菌学学报,19(3):344 - 349。采用免疫电镜(immuno-EM)技术对酿酒酵母菌和植物寄生物假尿菌不同内质网(ER)亚室中携带His-Asp-Glu-Leu (HDEL)蛋白进行了定量分析。在这两种真菌中,内质网内这些蛋白质的免疫金标记是核膜内的三倍。在豆芽联合杆菌中,萌发的尿素孢子中的内质网与植物内部产生的真菌结构(如吸器)中的内质网不同。在吸器中,蓄水池内质网分化出大管泡复合物(TVC)。TVC比普通内质网池含有更高水平的含hdl蛋白。ELISA读数还表明,与萌发的尿道孢子相比,分离的吸器中这些蛋白质的浓度增加。在酿酒酵母中,内质网分化为皮质区和内区。免疫电镜显示结合蛋白(BiP)的标记在细胞皮层的内质网中较低。热休克增加了BiP信号,但内质网内的相对分布没有变化。我们的研究结果表明,内质网亚室可以通过免疫金标记具有保留信号的蛋白质来区分。在特殊情况下,例如在锈菌的寄生阶段,这些蛋白质在内质网亚室中积累到更高的水平,可能是对植物诱导的胁迫的反应。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Endoplasmic Reticulum Subcompartments in a Plant Parasitic Fungus and in Baker's Yeast: Differential Distribution of Lumenal Proteins

Bachem, U., and Mendgen, K. 1995. ER subcompartments in a plant parasitic fungus and in baker's yeast: Differential distribution of lumenal proteins. Experimental Mycology 19, 137-152. His-Asp-Glu-Leu (HDEL)-bearing proteins were quantified in different endoplasmic reticulum (ER) subcompartments of Saccharomyces cerevisiae and the plant parasite Uromyces viciae-fabae by immuno-electron microscopy (immuno-EM). In both fungi, the immunogold labeling of these proteins within the ER was three times greater than within the nuclear envelope. In U. viciae-fabae, the ER in germinating uredospores differed from the ER in fungal structures produced within the plant, e.g., haustoria. In haustoria, the cisternal ER differentiated large tubular-vesicular complexes (TVC). TVC contained higher levels of HDEL-bearing proteins than ordinary ER cisternae. ELISA readings also indicated an increased concentration of these proteins in isolated haustoria compared to germinating uredospores. In S. cerevisiae, the ER was differentiated into cortical and internal regions. Immuno-EM revealed that labeling of the binding protein (BiP) was lower in the ER of the cell cortex. Heat shock increased BiP signals, but the relative distribution within the ER did not change. Our results suggest that ER subcompartments can be differentiated by immunogold labeling of proteins with a retention signal. In special cases, such as in the parasitic phase of rust fungi, these proteins accumulate to higher levels in ER subcompartments, probably as a response to plant-induced stress.

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