The J- and G/F-domains of the majorSynechocystisDnaJ protein Sll0897 are sufficient for cell viability but not for heat resistance

被引:2
作者
Dueppre, Eva [1 ]
Schneider, Dirk [1 ]
机构
[1] Johannes Gutenberg Univ Mainz, Biochem, Dept Chem, Johann Joachim Becher Weg 30, D-55128 Mainz, Germany
来源
FEBS OPEN BIO | 2020年 / 10卷 / 11期
关键词
chaperone; cyanobacteria; DnaJ; Hsp40; stress response; Synechocystis; DNAK MULTIGENE FAMILY; ESCHERICHIA-COLI; HSP40; YDJ1; HSP70; IDENTIFICATION; CONFORMATION; BINDING; REGION; GENES;
D O I
10.1002/2211-5463.12980
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 cyanobacteriumSynechocystissp. PCC6803. The expression of the N-terminally located J- and G/F-domains is essential and sufficient for the proteins' fundamentalin vivofunctions, whereas the presence of the full-length protein, containing the C-terminal substrate-binding domains, is crucial under stress conditions.
引用
收藏
页码:2343 / 2349
页数:7
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