dos Santos C F, Larson R E, Panek A D, Paschoalin V M
Depto. de Bioquímica, Universidade Federal do Rio de Janeiro, Cidade Universitária, Brasil.
Biochem Mol Biol Int. 1997 Feb;41(2):359-66. doi: 10.1080/15216549700201371.
Soluble calmodulin-binding proteins from Saccharomyces carlsbergensis were analyzed in cells grown on glucose, maltose and galactose as carbon source. A large number of polypeptide chains showed affinity for calmodulin by affinity chromatography and overlay techniques. Amongst these, polypeptides of 115, 67 and 45 kDa were only detected during the second exponential phase of growth on glucose or non-fermentative carbon sources, suggesting that they might be subjected to catabolite repression. Polypeptides of 195 and 22 kDa were only observed in cells grown on maltose, whereas 88 kDa polypeptide was only observed in galactose-grown cells. Among the calmodulin -binding polypeptides, eight were phosphorylated in a Ca2+/calmodulin -dependent manner (220, 200, 175, 100, 62, 55, 31 and 16 kDa). Ca2+/calmodulin dependent [gamma-32P] incorporation was dramatically decreased in yeast cells submitted to a heat treatment.
对以葡萄糖、麦芽糖和半乳糖作为碳源生长的卡尔斯伯酵母中的可溶性钙调蛋白结合蛋白进行了分析。通过亲和层析和覆盖技术,大量的多肽链显示出对钙调蛋白的亲和力。其中,115、67和45 kDa的多肽仅在以葡萄糖或非发酵性碳源生长的第二个指数生长期被检测到,这表明它们可能受到分解代谢物阻遏。195和22 kDa的多肽仅在以麦芽糖生长的细胞中观察到,而88 kDa的多肽仅在以半乳糖生长的细胞中观察到。在钙调蛋白结合多肽中,有8种以Ca2+/钙调蛋白依赖性方式被磷酸化(220、200、175、100、62、55、31和16 kDa)。在经过热处理的酵母细胞中,Ca2+/钙调蛋白依赖性的[γ-32P]掺入显著减少。