Division of Bioscience and Bioinformatics, College of Natural Science, Myongji University, Gyeonggi-Do, Korea.
J Antibiot (Tokyo). 2011 Jan;64(1):97-101. doi: 10.1038/ja.2010.148. Epub 2010 Dec 8.
Streptomycetes are the major natural source of clinical antibiotics. The enhanced secondary metabolite production of many streptomycetes by S-adenosylmethionine (SAM) in previous studies suggested the existence of a common SAM regulatory effect. We screened nine proteins using the phosphoprotein purification column from Streptomyces coelicolor. Among them, genes (SCO5477, SCO5113, SCO4647, SCO4885 and SCO1793) for five proteins were disrupted by insertion mutation. The undecylprodigiosin and actinorhodin productions were changed in all mutations. The SAM-induced enhancement of actinorhodin production was abolished by all mutations except SCO4885 mutation, which reduced the production of actinorhodin and undecylprodigiosin with SAM treatment. This study demonstrates that phosphoprotein affinity purification can be used as a screening method to identify the proteins involved SAM signaling.
链霉菌是临床抗生素的主要天然来源。先前的研究表明，S-腺苷甲硫氨酸（SAM）可增强许多链霉菌的次生代谢产物的产生，这表明存在一种常见的 SAM 调节效应。我们使用来自变铅青链霉菌的磷酸蛋白纯化柱筛选了 9 种蛋白质。其中，有 5 种蛋白质的基因（SCO5477、SCO5113、SCO4647、SCO4885 和 SCO1793）通过插入突变被破坏。所有突变都改变了乌地那非和放线紫红素的产生。除了 SCO4885 突变之外，所有突变都消除了 SAM 诱导的放线紫红素产生的增强，而 SCO4885 突变降低了 SAM 处理时放线紫红素和乌地那非的产生。本研究表明，磷酸蛋白亲和纯化可用作筛选方法来鉴定参与 SAM 信号的蛋白质。
