Larsen A, Sypherd P
Mol Gen Genet. 1979 Aug;175(1):99-109. doi: 10.1007/BF00267861.
Ribosomal proteins of the dimorphic fungus Mucor racemosus were isolated and characterized by 2-dimensional gel electrophoresis. Proteins from ribosomes of the yeast and mycelial phase were compared, and were found to be qualitatively indistinguishable. The only consistent difference in the patterns of proteins was in a protein of the 40S subunit, S-6. This protein was phosphorylated in yeast and hyphae forms, but not in asexual sporangiospores. Studies on protein S-6 showed that it contained 3 phosphate residues per molecule of protein when maximally phosphorylated. In this form 3 different tryptic peptides were shown to contain a single phosphoserine. The S-6 protein also existed in forms containing 1 or 2 phosphates per molecule, depending on growth conditions.
对双态真菌总状毛霉的核糖体蛋白进行了分离，并通过二维凝胶电泳对其进行了表征。比较了酵母和菌丝体阶段核糖体中的蛋白质，发现它们在质量上无法区分。蛋白质模式中唯一一致的差异在于40S亚基的一种蛋白质，即S-6。这种蛋白质在酵母和菌丝体形式中被磷酸化，但在无性孢子囊中未被磷酸化。对蛋白质S-6的研究表明，当最大程度磷酸化时，每分子蛋白质含有3个磷酸残基。在这种形式下，3种不同的胰蛋白酶肽显示含有单个磷酸丝氨酸。S-6蛋白还存在每分子含有1个或2个磷酸盐的形式，这取决于生长条件。
