Molecular characterization of DnaK from the halotolerant cyanobacterium Aphanothece halophytica for ATPase, protein folding, and copper binding under various salinity conditions

Plant Molecular Biology

Volumn 40, Issue 3, 1999, Pages 409-418

  Hibino, Takashi ^a   Kaku, Nobuo ^a   Yoshikawa, Hirofumi ^b   Takabe, Tetsuko ^c   Takabe, Teruhiro ^a  

^a MEIJO UNIVERSITY   (Japan)

^b TOKYO UNIVERSITY OF AGRICULTURE   (Japan)

^c NAGOYA UNIVERSITY   (Japan)

Author keywords

Aphanothece halophytica; ATPase; Chaperones; DnaK; Plastocyanin; Salt tolerance

Indexed keywords

ADENOSINE TRIPHOSPHATASE; APOPLASTOCYANIN; CARBOXY TERMINAL SEQUENCE; COPPER; DELETION MUTAGENESIS; ENZYME ACTIVITY; LACTATE DEHYDROGENASE; POTASSIUM CHLORIDE; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; SALINITY; SODIUM CHLORIDE;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; COPPER; CYANOBACTERIA; DNA PRIMERS; ESCHERICHIA COLI PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN FOLDING; SALTS; SEQUENCE HOMOLOGY, AMINO ACID;

APHANOTHECE HALOPHYTICA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; SYNECHOCOCCUS; SYNECHOCOCCUS ELONGATUS PCC 7942; SYNECHOCOCCUS SP.;

EID: 0033150135     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006273124726     Document Type: Article

References (29)

1. Badcoe, I.G., Smith, C.J., Halsall, D.J., Holbrook, J.J., Lund, P. and Clark, A.R. 1991. Binding of a chaperonin to the folding intermedidates of lactose dehydrogenase. Biochemistry 30: 9195-9200.
2. Bardwell, J.C.A. and Craig, E.A. 1984. Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proc. Natl. Acad. Sci. USA 81: 848-852.
3. Bhagwat, A.A. and Apte, S.K. 1989. Comparative analysis of proteins induced by heat shock, salinity, and osmotic stress in the nitrogen-fixing cyanobacterium Anabaena sp. strain L-31. J. Bact. 171: 5187-5189.
4. Boston, R.S., Vitanen, RV. and Vierling, E. 1996. Molecular chaperones and protein folding in plants. Plant Mol. Biol. 32: 191-222.
5. Bukau, B. and Horwich, A.L. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
6. Chitnis, P.R. and Nelson, N. 1991. Molecular cloning of the genes encoding two chaperone proteins of the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem. 266: 58-65.
7. de Boer, A.D. and Weisbeek, P.J. 1991. Chloroplast protein topogenesis: import, sorting and assembly. Biochim. Biophys. Acta. 1071: 221-253.
8. Flaherty, K.M., Deluca-Flaherty, C. and McKay, D.B. 1990. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346: 623-628.
9. Geladopoulos, T.P., Sotiroudis, T.G. and Evangelopoulos, A.E. 1991. A malachite green colorimetric assay for protein phosphatase activity. Anal. Biochem. 192: 112-116.
10. Gupta, R.S. and Golding, G.B. 1993. Evolution of Hsp70 gene and its implications regarding relationships between archaebacteria, eubacteria, and eukaryotes. J. Mol. Evol. 37: 573-582.
11. Harrison, C.J., Hayer-Hartl, M., Di Liberto, M., Haitl, F.U. and Kuriyan, J. 1997. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276: 431-435.
12. Haitl, F.U. 1996. Molecular chaperones in cellular protein folding. Nature 381: 571-580.
13. Hibino, T., de Boer, A.D., Weisbeek, P.J. and Takabe, T 1991. Reconstitution of mature plastocyanin from precursor apoplastocyanin expressed in Escherichia coli. Biochim. Biochys Acta 1058: 107-112.
14. Hibino, T., Lee, B.H. and Takabe, T 1994. Role of transit peptide seqence of plastocyanin for its expression, processing, and copper-binding activity in Escherichia coli. J. Biochem. 116: 826-832.
15. Hibino, T., Lee, B.H., Takabe, T. and Takabe, T. 1995. Expression and characterization of Met92Gln mutant plastocyanin from Silene pratensis. J. Biochem. 117: 101-106.
16. Iwasak, Y., Ishikawa, H., Hibino, T. and Takabe, T. 1991. Characterization of genes that encode subunits of cucumber PSI complex by N-terminal sequencing. Biochim. Biophys. Acta 1059: 141-148.
17. Kaneko, T., Tanaka, A., Sato, S., Kotani, H., Sazuka, T., Miyajima, N., Sugiura, M. and Tabata, S. 1995. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. I. Sequence features in the 1 Mb region from map positions of 64% to 92% of the genome. DNA Res. 2: 153-166.
18. Lee, B.H., Hibino, T., Jo, J., Viale, A.M. and Takabe, T. 1997. Isolation and characterization of dnaK genomic locus in a halotolerant cyanobacterium Aphanothece halophytica. Plant Mol. Biol. 35: 763-775.
19. McMillin, D.R., Rosenberg, R.C. and Gray, H.B. 1974. Preparation and spectroscopic studies of cobalt(II) derivatives of blue copper proteins. Proc. Natl. Acad. Sci. USA 71: 4760-4762.
20. Nimura, K., Yoshikawa, H. and Takahashi, H. 1994a. Identification of dnaK multigene family in Synechococcus sp. PCC 7942. Biochem. Biophys. Res. Commun. 201: 466-471.
21. Nimura, K., Yoshikawa, H. and Takahashi, H. 1994b. Sequence analysis of the third dnaK homolog gene in Synechococcus sp. PCC 7942. Biochem. Biophys. Res. Commun. 201: 848-854.
22. Nimura, K., Yoshikawa, H. and Takahashi, H. 1996. DnaK3, one of the three DnaK proteins of cyanobacterium Synechococcus sp. PCC7942, is quantitatively detected in the thylakoid membrane. Biochem. Biophys. Res. Commun. 229: 334-340.
23. Pierpaoli, E.V., Sandmeier, E., Baici, A., Schonfeld, H.J., Gisler, S. and Christen, P. 1997. The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system. J. Mol. Biol. 269: 757-768.
24. Rudiger, S., Buchberger, A. and Bukau, B. 1997. Interaction of Hsp70 chaperones with substrates. Nature Struct. Biol. 4: 342-349.
25. Slater, M.R. and Craig, E.A. 1989. The SSA1 and SSA2 genes of the yeast Saccharomyces cerevisiae. Nucl. Acids Res. 17: 805-806.
26. Webb, R. and Sherman, L. 1996. The cyanobacterial heat-shock response and the molecular chaperones. In: D.A. Bryant (Ed.), The Molecular Biology of Cyanobacteria, Kluwer Academic Publishers, Dordrecht, Netherlands, pp. 751-767.
27. Wetzstein, M., Volker, U., Dedio, J., Lobau, S., Zuber, U., Schiesswohl, M.S., Herget, C., Hecker, M. and Schumann, W. 1992. Cloning, sequencing, and molecular analysis of the dnaK locus from Bacillus subtilis. J Bact. 174: 3300-3310.
28. Wilbanks, S.M. and McKay, D.B. 1995. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem. 270: 2251-2257.
29. Zhu, X., Zhao, X., Burkholder, W.F., Gragerov, A., Ogata, C.M., Gottesman, M. and Hendrickson, W.A. 1996. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272: 1606-1614.