Gentry D R, Cashel M
Section on Molecular Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
J Bacteriol. 1995 Jul;177(13):3890-3. doi: 10.1128/jb.177.13.3890-3893.1995.
The SpoT protein of Escherichia coli serves as a source of degradation as well as an apparent source of synthesis of (p)ppGpp. Since the subcellular localization of SpoT might be a clue to its function, we have used SpoT-specific antisera to analyze cell extracts fractionated on sucrose gradients. We find that the SpoT protein is not bound to ribosomes or to either inner or outer membrane fractions. Although the SpoT protein is found in large aggregates, its localization is probably cytosolic.
大肠杆菌的SpoT蛋白是（p）ppGpp降解的来源，也是其明显的合成来源。由于SpoT的亚细胞定位可能是其功能的一个线索，我们使用SpoT特异性抗血清来分析在蔗糖梯度上分级分离的细胞提取物。我们发现SpoT蛋白不与核糖体结合，也不与内膜或外膜组分结合。尽管SpoT蛋白以大聚集体形式存在，但其定位可能是在胞质溶胶中。
