Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 65, 2001 - Issue 10
Journal homepage
83
Views
14
CrossRef citations to date
0
Altmetric
Original Articles

Characterization of Nucleoside Diphosphate Kinase from Moderately Halophilic Eubacteria

Yasushi YONEZAWALaboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University
,
Hiroko TOKUNAGALaboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University
,
Matsujiro ISHIBASHILaboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University
&
Masao TOKUNAGALaboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University
Pages 2343-2346 | Received 23 Apr 2001, Accepted 24 May 2001, Published online: 22 May 2014

  • 1) Tokunaga, M., Matsuoka, K., and Tokunaga, H., Identification and NH2-terminal amino acid sequences of DnaK and GroEL homologues in moderate eubacterial halophiles. Biosci. Biotechnol. Biochem., 61, 1388-1390 (1997).
  • 2) Tokunaga, M., Miyawaki, H., Shiraishi, Y., and Tokunaga, H., Purification and characterization of a GroEL homologue from the moderately eubacterial halophile Pseudomonas sp. #43. FEMS Microbiol. Lett., 152, 321-326 (1997).
  • 3) Tokunaga, H., Hara, S., Arakawa, T., Ishibashi, M., Gupta, R.S., and Tokunaga, M., Identification and partial purification of DnaK homologue from extremely halophilic archaebacteria, Halobacterium cutirubrum. J. Prot. Chem., 18, 837-844 (1999).
  • 4) Ishibashi, M., Tokunaga, H., Hiratsuka, K., Yonezawa, Y., Tsurumaru, H., Arakawa, T., and Tokunaga, M., NaCl-activated nucleoside diphosphate kinase from extremely halophilic archaeon, Halobacterium salinarum, maintains native conformation without salt. FEBS Lett., 493, 134-138 (2001).
  • 5) Kushner, D.J., Life in high salt and solute concentrations: halophilic bacteria. In Microbial Life in Extreme Environments. ed. D.J. Kushner, Academic Press, London, pp. 317-368 (1978).
  • 6) Kushner, D. and Kamekura, M., Physiology of halophilic eubacteria. In Halophilic bacteria. volI. ed. F. Rodrigues-Velera. CRC Press, pp. 109-138 (1988).
  • 7) Lanyi, J.K., Salt-dependent properties of proteins from extremely halophilic bacteria. Bacteriol. Rev., 38, 272-290 (1974).
  • 8) Kamekura, M., Production and function of enzymes of eubacterial halophiles. FEMS Microbiol. Rev., 39, 145-150 (1986).
  • 9) Ventosa, A., Nieto, J., and Oren, A., Biology of moderately halophilic aerobic bacteria. Microbiol. Mol. Biol. Rev., 62, 504-544 (1998).
  • 10) Pearson, W.R. and Lipman, D.J., Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA, 85, 2444-2448 (1988).
  • 11) Agarwal, R.P. and Parks, R.E., Jr., Erythrocytic nucleoside diphosphokinase. V. Some properties and behavior of the pI7.3 isozyme. J. Biol. Chem., 246, 2258-2264 (1971).
  • 12) Dym, O., Mevarech, M., and Sussman, J.L., Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science, 267, 1344-1346 (1995).
  • 13) Salvarrey, M.S. and Cazzulo, J.J., Some properties of the NADP-specific malic enzyme from the moderate halophile Vibrio costicola. Can. J. Microbiol., 26, 50-57 (1980).
  • 14) Harry, K., Sharma, N., and Fitt, P.S., Preparation and properties of highly-purified Vibrio costicola polynucleotide phosphorylase. Biochim. Biophys. Acta, 828, 29-38 (1985).
  • 15) Ahonkhai, I., Kamekura, M., and Kushner, D.J., Effects of salts on the aspartate transcarbamylase of a halophilic eubacterium, Vibrio costicola. Biochem. Cell Biol., 67, 666-669 (1989).
  • 16) Mevarech, M., Frolow, F., and Gloss, L.M., Halophilic enzymes: proteins with a grain of salt. Biophys. Chem., 86, 155-164 (2000).
  • 17) Danson, M.J. and Hough, D.W., The structure basis of protein halophilicity. Comp. Biochem. Physiol., 117A, 307-312 (1997).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.