Lakhotia S C, Singh B N
Department of Zoology, Banaras Hindu University, Varanasi, India.
Experientia. 1996 Aug 15;52(8):751-6. doi: 10.1007/BF01923984.
A homologue of the chaperonin protein of the HSP60 family has not been shown so far in Drosophila. Using an antibody specific to HSP60 family protein in Western blotting and immunocytochemistry, we showed that a 64-kDa polypeptide, homologous to the HSP60, is constitutively present in all tissues of Drosophila melanogaster throughout the life cycle from the freshly laid egg to all embryonic, larval and adult stages. A 64-kDa polypeptide reacting with the same antibody in Western blots is present in all species of Drosophila examined. Using Western blotting in conjunction with 35S-methionine labeling of newly synthesized proteins and immuno-precipitation of the labeled proteins with HSP60-specific antibody, it was shown that synthesis of the 64-kDa homologue of HSP60 is appreciably increased by heat shock only in the Malpighian tubules, which are already known to lack the common HSPs.
迄今为止，尚未在果蝇中发现HSP60家族伴侣蛋白的同源物。通过在蛋白质免疫印迹法和免疫细胞化学中使用对HSP60家族蛋白特异的抗体，我们发现一种与HSP60同源的64 kDa多肽，在黑腹果蝇从新鲜产下的卵到所有胚胎、幼虫和成虫阶段的整个生命周期中，在其所有组织中持续存在。在所有检测的果蝇物种中，都存在一种在蛋白质免疫印迹法中与相同抗体发生反应的64 kDa多肽。通过结合使用蛋白质免疫印迹法与新合成蛋白质的35S-甲硫氨酸标记，以及用HSP60特异性抗体对标记蛋白质进行免疫沉淀，结果表明，仅在已知缺乏常见热休克蛋白的马氏管中，热休克可显著增加HSP60的64 kDa同源物的合成。
