0000000000318925
AUTHOR
Eva Düppre
Similarities and singularities of three DnaK proteins from the cyanobacterium Synechocystis sp. PCC 6803.
In the genome of completely sequenced mesophilic cyanobacterium Synechocystis sp. PCC 6803 three DnaK proteins are encoded, which share a high degree of sequence identity in their N-terminal ATPase region as well as in the adjacent peptide-binding domain. However, as typical for DnaK proteins, the C-termini of the three Synechocystis proteins are highly diverse. To study the functions of the three Synechocystis DnaK proteins in more detail, we have analyzed the abundance of the individual proteins in Synechocystis cells as well as dnaK expression under various stress conditions. The presented results show that all three Synechocystis DnaK proteins interact with the same GrpE nucleotide exch…
Specific and promiscuous functions of multiple DnaJ proteins in Synechocystis sp. PCC 6803
Cyanobacterial genomes typically encode multiple Hsp70 (DnaK) and Hsp40 (DnaJ) chaperones, and in the genome of the cyanobacteriumSynechocystisPCC 6803, three DnaK proteins are encoded together with seven DnaJ proteins. While only two of the DnaJ proteins can complement the growth defect of anEscherichia coliΔdnaJstrain, only disruption of thednaJgenesll0897resulted in a growth defect at elevated temperatures. Based on the domain structure and the phenotype observed following disruption of the encoding gene, Sll0897 can be classified as a canonical heat-shock protein inSynechocystis. Furthermore, mostdnaJgenes could be deleted individually, whereas disruption of the gene encoding the DnaJ S…