6533b7d8fe1ef96bd126a30d
RESEARCH PRODUCT
Similarities and singularities of three DnaK proteins from the cyanobacterium Synechocystis sp. PCC 6803.
Eva DüppreEva DüppreDirk SchneiderDirk SchneiderEva Rupprechtsubject
Physiologygenetic processesAmino Acid MotifsMolecular Sequence DataSequence alignmentPlant SciencePlasma protein bindingBiologymedicine.disease_causeMicrobiologyConserved sequenceNucleotide exchange factorBacterial ProteinsStress PhysiologicalmedicineHSP70 Heat-Shock ProteinsAmino Acid SequencePeptide sequenceConserved SequenceHeat-Shock ProteinsMutationSynechocystisSynechocystisCell BiologyGeneral MedicineGene Expression Regulation Bacterialbiology.organism_classificationBiochemistrybiological sciencesMutationbacteriaSequence AlignmentFunction (biology)Protein Bindingdescription
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 exchange factor. A comparative analysis indicates that DnaK2 is the most abundant DnaK protein in Synechocystis cells and only the expression of dnaK2 is highly up-regulated under various stress conditions. Finally, we show that a small amino acid motif, which is typically conserved at the very C-terminus of cyanobacterial DnaK3 proteins, is essential for the DnaK3 in vivo function.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2010-05-13 | Plantcell physiology |