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The J- and G/F-domains of the major Synechocystis DnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance.
FEBS Open Bio ( IF 2.6 ) Pub Date : 2020-09-23 , DOI: 10.1002/2211-5463.12980
Eva Düppre 1 , Dirk Schneider 1
Affiliation  

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.

中文翻译:

主要集胞藻 DnaJ 蛋白 Sll0897 的 J 和 G/F 结构域足以维持细胞活力,但不具备耐热性。

Hsp70 蛋白及其 Hsp40 辅助伴侣是原核生物和真核生物中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,以确定蓝藻集胞藻属的主要 Hsp40/DnaJ 蛋白 Sll0897 的关键功能所需的蛋白质结构域。PCC6803。N 末端的 J 和 G/F 结构域的表达对于蛋白质的基本体内功能是必不可少的,而包含 C 末端底物结合结构域的全长蛋白质的存在是在压力条件下至关重要。
更新日期:2020-11-04
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