Vorderwülbecke S, Kramer G, Merz F, Kurz T A, Rauch T, Zachmann-Brand B, Bukau B, Deuerling E
Ciphergen Biosystems GmbH, Hannah-Vogt-Str.1, 37085 Göttingen, Germany.
FEBS Lett. 2004 Feb 13;559(1-3):181-7. doi: 10.1016/S0014-5793(04)00052-3.
Escherichia coli trigger factor (TF) and DnaK cooperate in the folding of newly synthesized proteins. The combined deletion of the TF-encoding tig gene and the dnaK gene causes protein aggregation and synthetic lethality at 30 degrees C. Here we show that the synthetic lethality of DeltatigDeltadnaK52 cells is abrogated either by growth below 30 degrees C or by overproduction of GroEL/GroES. At 23 degrees C DeltatigDeltadnaK52 cells were viable and showed only minor protein aggregation. Overproduction of GroEL/GroES, but not of other chaperones, restored growth of DeltatigDeltadnaK52 cells at 30 degrees C and suppressed protein aggregation including proteins >/=60 kDa, which normally require TF and DnaK for folding. GroEL/GroES thus influences the folding of proteins previously identified as DnaK/TF substrates.
大肠杆菌触发因子(TF)和 DnaK 在新合成蛋白质的折叠过程中协同作用。编码 TF 的 tig 基因和 dnaK 基因的联合缺失会导致蛋白质聚集,并在 30℃时产生合成致死性。在此我们表明,DeltatigDeltadnaK52 细胞的合成致死性可通过在 30℃以下生长或通过过量表达 GroEL/GroES 来消除。在 23℃时,DeltatigDeltadnaK52 细胞能够存活,且仅表现出轻微的蛋白质聚集。过量表达 GroEL/GroES(而非其他伴侣蛋白)可恢复 DeltatigDeltadnaK52 细胞在 30℃时的生长,并抑制蛋白质聚集,包括那些分子量≥60 kDa 的蛋白质,这些蛋白质通常需要 TF 和 DnaK 来进行折叠。因此,GroEL/GroES 影响了先前被鉴定为 DnaK/TF 底物的蛋白质的折叠。