Martin F, Requena J M, Martin J, Alonso C, López M C
Instituto de Parasitología Lopez Neyra CSIC, Granada, Spain.
Biochem Biophys Res Commun. 1993 Nov 15;196(3):1155-62. doi: 10.1006/bbrc.1993.2372.
The present study provides immunological evidence of the constitutive presence of the Hsp70 protein in the cytoplasm of logarithmically growing T. cruzi parasites cultured at the normal temperature of 28 degrees C and of the translocation of the protein to the nucleus upon a heat shock treatment (2 hours at 37 degrees C). The nuclear translocation of the protein must depend on other factors beside the temperature per se since at 28 degrees C, in stationary phase growing parasites, the Hsp70 protein was present in both the cytoplasm and the nucleus. During recovery at 28 degrees C the protein leaves the nuclei but the nuclear-cytoplasmic translocation of the protein is a much more gradual process than its initial transport to the nucleus. Since the isoform of the nuclear Hsp70 is different from that found in the cytoplasm it is likely that before translocation to the nucleus the cytoplasmic Hsp70 nuclear precursor must undergo a specific modification.
本研究提供了免疫证据,证明在28℃常温下培养的对数生长期克氏锥虫寄生虫细胞质中组成性存在Hsp70蛋白,以及热休克处理(37℃处理2小时)后该蛋白向细胞核的转位。该蛋白的核转位必定除了温度本身之外还依赖于其他因素,因为在28℃处于稳定期生长的寄生虫中,Hsp70蛋白同时存在于细胞质和细胞核中。在28℃恢复过程中,该蛋白离开细胞核,但蛋白的核质转位过程比其最初转运到细胞核的过程要缓慢得多。由于细胞核Hsp70的同工型与细胞质中发现的不同,因此细胞质Hsp70核前体在转位到细胞核之前很可能必须经历特定修饰。