Bukau B, Reilly P, McCarty J, Walker G C
Zentrum für Molekulare Biologie, Universität Heidelberg, FRG.
J Gen Microbiol. 1993 Jan;139(1):95-9. doi: 10.1099/00221287-139-1-95.
Previously reported cell fractionation experiments have yielded conflicting information on the cellular localization of the DnaK heat shock protein of Escherichia coli. Here we used immunogold labelling of ultra-thin sections to determine the localization of DnaK in unstressed cells at 30 degrees C as well as in heat-shocked cells. In cells grown at 30 degrees C, gold particles were found predominantly in the cytoplasm, indicating that the majority of the DnaK molecules are cytoplasmic; however, a fraction of the gold particles was located in proximity to the membranes, raising the possibility that a subpopulation of DnaK proteins is membrane-associated. Heat shock of the cells did not induce detectable relocalization of DnaK.
先前报道的细胞分级分离实验,就大肠杆菌DnaK热休克蛋白的细胞定位得出了相互矛盾的信息。在此,我们利用超薄切片的免疫金标记法,来确定DnaK在30摄氏度未受应激的细胞以及热休克细胞中的定位。在30摄氏度培养的细胞中,金颗粒主要见于细胞质中,这表明大多数DnaK分子存在于细胞质中;然而,有一部分金颗粒位于靠近细胞膜处,这增加了DnaK蛋白亚群与膜相关的可能性。细胞热休克并未诱导DnaK发生可检测到的重新定位。