Mitchell C, Vary J C
Department of Biochemistry, University of Illinois, Chicago 60612.
J Bacteriol. 1989 Jun;171(6):2915-8. doi: 10.1128/jb.171.6.2915-2918.1989.
During sporulation of Bacillus subtilis, several proteins were shown to interact with GTP in specific ways. UV light was used to cross-link [alpha-32P]GTP to proteins in cell extracts at different stages of growth. After electrophoresis, 11 bands of radioactivity were found in vegetative cells, 4 more appeared during sporulation, and only 9 remained in mature spores. Based on the labeling pattern with or without UV light to cross-link either [alpha-32P]GTP or [gamma-32P]GTP, 11 bands of radioactivity were apparent guanine nucleotide-binding proteins, and 5 bands appeared to be phosphorylated and/or guanylated. Similar results were found with Bacillus megaterium. Assuming that GTP might be a type of signal for sporulation, it could interact with and regulate proteins by at least three mechanisms.
在枯草芽孢杆菌的芽孢形成过程中，有几种蛋白质被证明以特定方式与GTP相互作用。利用紫外线将[α-32P]GTP与处于不同生长阶段的细胞提取物中的蛋白质进行交联。电泳后，在营养细胞中发现了11条放射性条带，芽孢形成过程中又出现了4条，而在成熟孢子中仅剩下9条。根据用紫外线交联[α-32P]GTP或[γ-32P]GTP与否的标记模式，11条放射性条带明显是鸟嘌呤核苷酸结合蛋白，5条条带似乎发生了磷酸化和/或鸟苷酸化。巨大芽孢杆菌也得到了类似结果。假设GTP可能是芽孢形成的一种信号类型，它可能通过至少三种机制与蛋白质相互作用并对其进行调节。
