title: Specific and promiscuous functions of multiple DnaJ proteins in Synechocystis sp. PCC 6803.
abstract: Cyanobacterial genomes typically encode multiple Hsp70 (DnaK) and Hsp40 (DnaJ) chaperones, and in the genome of the cyanobacterium Synechocystis PCC 6803, three DnaK proteins are encoded together with seven DnaJ proteins. While only two of the DnaJ proteins can complement the growth defect of an Escherichia coli ΔdnaJ strain, only disruption of the dnaJ gene sll0897 resulted 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 in Synechocystis. Furthermore, most dnaJ genes could be deleted individually, whereas disruption of the gene encoding the DnaJ Sll1933 failed, which suggests an essential, yet undefined, function for Sll1933. Since after deletion of the remaining dnaJ genes the phenotypes were not altered, the functions of these DnaJs either are not critical or are taken over by the remaining DnaJs. Nevertheless, only the two dnaJ genes sll0909 and sll1384 could be disrupted in combination, suggesting physiological functions for the two encoded proteins which either are not overlapping and/or can be fulfilled by the remaining DnaJs in the double-disruption strain. Taken together, the present analysis indicates specific and promiscuous functions for multiple DnaJ proteins in Synechocystis.
authors.affiliation: Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung (ZBMZ), Albert-Ludwigs-Universität Freiburg, Stefan-Meier-Strasse 19, 79104 Freiburg, Germany.|Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz, 55128 Mainz, Germany.
authors.forename: Eva
authors.initials: E
authors.lastname: Düppre
authors.affiliation: Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz, 55128 Mainz, Germany.
authors.forename: Eva
authors.initials: E
authors.lastname: Rupprecht
authors.affiliation: Institut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung (ZBMZ), Albert-Ludwigs-Universität Freiburg, Stefan-Meier-Strasse 19, 79104 Freiburg, Germany.|Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz, 55128 Mainz, Germany.
authors.forename: Dirk
authors.initials: D
authors.lastname: Schneider
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D050956:HSP40 Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005810:Multigene Family; D017434:Protein Structure, Tertiary; D046939:Synechocystis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D050956:HSP40 Heat-Shock Proteins