The overproduction of Synechocystis sp. PCC 6803 heat-shock protein (Sll0170) protects Escherichia coli against high-temperature stress

References

• Whitton BA, Potts M. The ecology of cyanobacteria: their diversity in time and space. Dordrecht: Kluwer Academic Publisher; 2000.
   Google Scholar
• Zhang Y, Niu X, Shi M, et al. Identification of a transporter Slr0982 involved in ethanol tolerance in cyanobacterium Synechocystis sp. PCC 6803. Front Microbiol. 2015;6:1–13.
   PubMedGoogle Scholar
• Suzuki I, Simon WJ, Slabas AR. The heat shock response of Synechocystis sp. PCC 6803 analysed by transcriptomics and proteomics. J Exp Bot. 2006;57:1573–1578.
   PubMed Web of Science ®Google Scholar
• Düppre E, Rupprecht E, Schneider D. Specific and promiscuous functions of multiple DnaJ proteins in Synechocystis sp. PCC 6803. Microbiology. 2011;157:1269–1278.
   PubMed Web of Science ®Google Scholar
• Kim J, Ahn M, Park Y, et al. Synechocystis PCC6803 and PCC6906 dnaK2 expression confers salt and oxidative stress tolerance in Arabidopsis via reduction of hydrogen peroxide accumulation. Mol Biol Rep. 2014;41:1091–1101.
   PubMed Web of Science ®Google Scholar
• Rupprecht E, Gathmann S, Fuhrmann E, et al. Three different DnaK proteins are functionally expressed in the cyanobacterium Synechocystis sp. PCC 6803. Microbiology. 2007;153:1828–1841.
   PubMed Web of Science ®Google Scholar
• Nakamoto H, Suzuki M, Kojima K. Targeted inactivation of the hrcA repressor gene in cyanobacteria. FEBS Lett. 2003;549:57–62.
   PubMed Web of Science ®Google Scholar
• Sato M, Nimura-Matsune K, Watanabe S, et al. Expression analysis of multiple dnaK genes in the cyanobacterium Synechococcus elongatus PCC 7942. J Bacteriol. 2007;189:3751–3758.
   PubMed Web of Science ®Google Scholar
• Nakamoto H, Fujita K, Ohtaki A, et al. Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins. J Biol Chem. 2014;289:6110–6119.
   PubMed Web of Science ®Google Scholar
• Rupprecht E, Düppre E, Schneider D. Similarities and singularities of three DnaK proteins from the cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Physiol. 2010;51:1210–1218.
   PubMed Web of Science ®Google Scholar
• Nimura K, Takahashi H, Yoshikawa H. Characterization of the dnaK multigene family in the cyanobacterium Synechococcus sp. strain PCC7942. J Bacteriol. 2001;183(4):1320–1328.
   PubMed Web of Science ®Google Scholar
• Mandel M, Higa A. Calcium-dependent bacteriophage DNA infection. J Mol Biol. 1970;53:159–162.
   PubMed Web of Science ®Google Scholar
• Fregel R, Rodriguez V, Cabrera VM. Microwave improved Escherichia coli transformation. Lett Appl Microbiol. 2008;46:498–499.
   PubMed Web of Science ®Google Scholar
• Aune TEV, Aachmann FL. Methodologies to increase the transformation efficiencies and the range of bacteria that can be transformed. Appl Microbiol Biotechnol. 2010;85:1301–1313.
   PubMed Web of Science ®Google Scholar
• Williams JGK. Construction of specific mutants in photosystem II photosynthetic reaction center by genetic engineering methods in Synechocystis 6803. Methods Enzymol. 1988;167:766–778.
   Web of Science ®Google Scholar
• Laemmli UK. Cleavage of structural proteins during the assembly of head of Bacteriophage T4. Nature. 1970;227:680–685.
   PubMed Web of Science ®Google Scholar
• Thompson JD, Higgins DG, Gibson TJ. CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994;22:4673–4680.
   PubMed Web of Science ®Google Scholar
• Zhou W, Zhou T, Li M-X, et al. The Arabidopsis J-protein AtDjB1 facilitates thermotolerance by protecting cells against heat-induced oxidative damage. New Phytologist. 2012;194:364–378.
   PubMed Web of Science ®Google Scholar
• Al-Whaibi MH. Plant heat-shock proteins: a mini review. J King Saud Univ – Sci. 2011;23:139–150.
   Google Scholar
• Itoh T, Matsuda H, Mori H. Phylogenetic analysis of the third Hsp70 homolog in Escherichia coli; a novel member of the Hsc66 subfamily and its possible co-chaperone. DNA Res. 1999;6:299–305.
   PubMedGoogle Scholar
• Liberek K, Galitski TP, Zylicz M, et al. The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the σ32 transcription factor. Proc Natl Acad Sci USA. 1992;89:3516–3520.
   PubMed Web of Science ®Google Scholar
• Horváth I, Glatz A, Nakamoto H, et al. Heat shock response in photosynthetic organisms: membrane and lipid connections. Prog Lipid Res. 2012;51:208–220.
   PubMed Web of Science ®Google Scholar
• Genevaux P, Georgopoulos C, Kelley WL. The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions. Mol Microbiol. 2007;66:840–857.
   PubMed Web of Science ®Google Scholar
• Hinault MP, Cuendet AFH, Mattoo RUH, et al. Stable β-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones. J Biol Chem. 2010;285:38173–38182.
   PubMed Web of Science ®Google Scholar
• Dörrich AK, Mitschke J, Siadat O, et al. Deletion of the Synechocystis sp. PCC 6803 kaiAB1C1 gene cluster causes impaired cell growth under light–dark conditions. Microbiology. 2014;160:2538–2550.
   PubMed Web of Science ®Google Scholar
• Mason CA, Dunner J, Indra P, et al. Heat-induced expression and chemically induced expression of the Escherichia coli stress protein HtpG are affected by the growth environment. Appl Environ Microbiol. 1999;3433–3440.
   PubMed Web of Science ®Google Scholar
• Paek KH, Walker GC. Escherichia coli dnaK null mutants are inviable at high temperature. J Bacteriol. 1987;169:283–290.
   PubMed Web of Science ®Google Scholar
• Nakamoto H. Molecular chaperones and stress tolerance in cyanobacteria. In: Srivastava AK, Rai AN, Neilan BA, editors. Stress biology of cyanobacteria: molecular mechanisms to cellular responses. Boca Raton (FL): CRC Press; 2013. p. 114–144.
   Google Scholar
• Rajaram H, Chaurasia A, Apte S. Cyanobacterial heat-shock response: role and regulation of molecular chaperones. Microbiology. 2014;160:647–658.
   PubMed Web of Science ®Google Scholar
• Bracher A, Verghese J. GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones. Sub-cellular Biochem. 2015;78:1–33.
   PubMedGoogle Scholar