Pinto M, Morange M, Bensaude O
Groupe de Biologie Moléculaire du Stress, Institut Pasteur, Paris, France.
J Biol Chem. 1991 Jul 25;266(21):13941-6.
Using beta-galactosidase and luciferase as reporter enzymes, we have previously shown that enzymatic inactivation occurring during a heat shock is concomitant with protein insolubilization (Nguyen, V. T., Morange, M., and Bensaude, O. (1989) J. Biol. Chem. 264, 10487-10492). In this paper, we observe that pretreatment of cells with D2O and glycerol, compounds known to stabilize protein structure, leads to a parallel decrease of protein inactivation and insolubilization, suggesting that these two phenomena result most probably from heat-induced protein denaturation. We found that heat shock-promoted inactivation and insolubilization are not irreversible processes, since even in the absence of protein synthesis, beta-galactosidase solubility and luciferase solubility and activity are recovered in vivo after a heat treatment. Cognate heat shock proteins might be involved in this renaturation process.
我们之前使用β-半乳糖苷酶和荧光素酶作为报告酶，发现热休克期间发生的酶失活与蛋白质不溶性化同时出现（阮，V.T.，莫朗热，M.，和本索德，O.（1989年）《生物化学杂志》264，10487 - 10492）。在本文中，我们观察到用重水和甘油预处理细胞，这两种已知能稳定蛋白质结构的化合物，会导致蛋白质失活和不溶性化同时平行降低，这表明这两种现象很可能是由热诱导的蛋白质变性引起的。我们发现热休克促进的失活和不溶性化不是不可逆过程，因为即使在没有蛋白质合成的情况下，热处理后β-半乳糖苷酶的溶解度以及荧光素酶的溶解度和活性在体内也会恢复。同源热休克蛋白可能参与了这个复性过程。
