Department of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, Germany.
FEBS Open Bio. 2020 Nov;10(11):2343-2349. doi: 10.1002/2211-5463.12980. Epub 2020 Sep 27.
Hsp70 proteins and their Hsp40 co-chaperones are essential components of cellular chaperone networks in both prokaryotes and eukaryotes. Here, we performed a genetic analysis to define the protein domains required for the key functions of the major Hsp40/DnaJ protein Sll0897 of the cyanobacterium Synechocystis sp. PCC6803. The expression of the N-terminally located J- and G/F-domains is essential and sufficient for the proteins' fundamental in vivo functions, whereas the presence of the full-length protein, containing the C-terminal substrate-binding domains, is crucial under stress conditions.
Hsp70 蛋白及其 Hsp40 共伴侣是原核生物和真核生物细胞伴侣网络的重要组成部分。在这里,我们进行了遗传分析,以确定蓝藻集胞藻 PCC6803 主要 Hsp40/DnaJ 蛋白 Sll0897 的关键功能所需的蛋白结构域。N 端定位的 J 结构域和 G/F 结构域的表达对于蛋白质的基本体内功能是必需和充分的,而全长蛋白(包含 C 端底物结合结构域)的存在在应激条件下是至关重要的。