6533b86ffe1ef96bd12cdad2
RESEARCH PRODUCT
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subject
0301 basic medicineCyanobacteriabiologyChemistryProtein domainSynechocystisbiology.organism_classificationDNAJ ProteinGenetic analysisGeneral Biochemistry Genetics and Molecular BiologyHsp70Cell biology03 medical and health sciences030104 developmental biology0302 clinical medicine030220 oncology & carcinogenesisChaperone (protein)biology.proteinViability assaydescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2020-09-27 | FEBS Open Bio |