Cloning, sequencing, and expression of a gene encoding the monomeric isocitrate dehydrogenase of the nitrogen-fixing bacterium, azotobacter vinelandii

Bioscience, Biotechnology and Biochemistry

Volumn 66, Issue 3, 2002, Pages 489-500

  Sahara, Takehiko ^a,b   Takada, Yasuhiro ^a   Takeuchi, Yoji ^a   Yamaoka, Naoto ^a   Fukunaga, Noriyuki ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

Azotobacter vinelandii; Isocitrate dehydrogenase gene; Nitrogen fixing bacterium

Indexed keywords

AZOTOBACTER; AZOTOBACTER VINELANDII; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PROKARYOTA;

BACTERIAL DNA; ISOCITRATE DEHYDROGENASE; PRIMER DNA;

5' UNTRANSLATED REGION; AMINO ACID SEQUENCE; ARTICLE; AZOTOBACTER VINELANDII; BACTERIOPHAGE; BIOSYNTHESIS; CULTURE MEDIUM; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; NORTHERN BLOTTING; NUCLEOTIDE SEQUENCE; PLASMID; PROMOTER REGION; SOUTHERN BLOTTING; WESTERN BLOTTING;

5' UNTRANSLATED REGIONS; AMINO ACID SEQUENCE; AZOTOBACTER VINELANDII; BACTERIOPHAGES; BASE SEQUENCE; BLOTTING, NORTHERN; BLOTTING, SOUTHERN; BLOTTING, WESTERN; CLONING, MOLECULAR; CULTURE MEDIA; DNA PRIMERS; DNA, BACTERIAL; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; ISOCITRATE DEHYDROGENASE; MOLECULAR SEQUENCE DATA; PLASMIDS; PROMOTER REGIONS (GENETICS);

EID: 0036490764     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.489     Document Type: Article

References (30)

1. Colman, R. F., Aspects of the structure and function of the isocitrate dehydrogenases. Pept. Protein Rev., 1, 41-69 (1983).
2. Fukunaga, N., Imagawa, S., Sahara, T., Ishii, A., and Suzuki, M., Purification and characterization of monomeric isocitrate dehydrogenase with NADP+-specificity from Vibrio parahaemolyticus Y-4. J. Biochem., 112, 849-855 (1992).
3. Suzuki, M., Sahara, T., Tsuruha, J., Takada, Y., and Fukunaga, N., Differential expression in Escherichia coli of the Vibrio sp. strain ABE-1 icdI and icdII genes encoding structurally different isocitrate dehydrogenase isozymes. J. Bacteriol.,177, 2138-2142 (1995).
4. Ishii, A., Imagawa, S., Fukunaga, N., Sasaki, S., Minowa, O., Mizuno, Y., and Shiokawa, H., Isozymes of isocitrate dehydrogenase from an obligately psychrophilic bacterium, Vibrio sp. strain ABE-1: Purification, and modulation of activities by growth conditions. J. Biochem., 102, 1489-1498 (1987).
5. Ochiai, T., Fukunaga, N., and Sasaki, S., Purification and some properties of two NADP+-specific isocitrate dehydrogenase from an obligately psychrophilic marine bacterium, Vibrio sp. strain ABE-1. J. Biochem., 86, 377-384 (1979).
6. Eikmanns, B. J., Rittmann, D., and Sahm, H., Cloning, sequence analysis, expression, and inactivation of the Corynebacterium glutamicum icd gene encoding isocitrate dehydrogenase and biochemical characterization of the enzyme. J. Bacteriol., 177, 774-782 (1995).
7. Stoddard, B. L., Dean, A. M., and Koshland, Jr., D. E., Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-A resolution: A pseudo-michaelis ternary complex. Biochemistry, 32, 9310-9316 (1993).
8. Hurley, J. H., Thorsness, P. E., Ramalingam, V., Helmers, N. H., Koshland, Jr., D. E., and Stroud, R. M., Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase. Proc. Natl. Acad. Sci., USA, 86, 8635-8639 (1989).
9. Hurley, J. H., Dean, A. M., Koshland, Jr., D. E., and Stroud, R. M., Catalytic mechanism of NADP + -dependent isocitrate dehydrogenase: Implications from the structures of magnesium-isocitrate and NADP+ complexes. Biochemistry, 30, 8671-8678 (1991).
10. of Azotobacter vinelandii. Biochim. Biophys. Acta, 191, 193-195 (1969).
11. Chung, A. E. and Franzen, J. S., Oxidized triphosphopyridine nucleotide specific isocitrate dehydrogenase from Azotobacter vinelandii: Isolation and characterization. Biochemistry, 8, 3175-3184 (1969).
12. Yates, M. G., Biochemistry of nitrogen fixation, In “The Biochemistry of Plants Vol. 5”, eds. Stumpf, P. K. and Conn, E. E., Academic Press, New York, pp. 1-64 (1980).
13. Edwards, D. J., Heinrikson, R. L., and Chung, A. E., Triphosphopyridine nucleotide specific isocitrate dehydrogenase from Azotobacter vinelandii. Alkylation of a specific methionine residue and amino acid sequence of the peptide containing this residue. Biochemistry, 13, 677-683 (1974).
14. Czerwinski, E. W., Bethge, P. H., Mathews, F. S., and Chung, A. E., A preliminary crystallographic study of isocitrate dehydrogenase from Azotobacter vinelandii. J. Mol. Biol., 115, 181-187 (1977).
15. Wilson, P. W. and Knight, S. G., “Experiments in bacterial physiology”, Burgess Publishing Co., Minnesota, p. 53 (1952).
16. Sambrook, J., Fritsch, E. F., and Maniatis, T., “Molecular cloning: A laboratory manual, 2nd ed.”, Cold Spring Harbor Laboratory Press, New York (1989).
17. Neidhardt, F. C., Bloch, P. L., and Smith, D. F., Culture media for enterobacteria. J. Bacteriol., 119, 736-749 (1974).
18. Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
19. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
20. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., “Current protocols in molecular biology”, John Wiley &Sons, Inc., New York (1987).
21. Grossberger, D., Minipreps of DNA from bacteriophage lambda. Nucleic Acids Res., 15, 6737 (1987).
22. Ishii, A., Suzuki, M., Sahara, T., Takada, Y., Sasaki, S., and Fukunaga, N., Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic bacterium, Vibrio sp. strain ABE-1. J. Bacteriol., 175, 6873-6880 (1993).
23. Rosenberg, M. and Court, D., Regulatory sequences involved in the promotion and termination of RNA transcription. Annu. Rev. Genet., 13, 319-353 (1979).
24. Ehretsmann, C. P., Carpousis, A. J., and Krisch, H. M., Specificity of Escherichia coli endoribonuclease RNase E: in vivo and in vitro analysis of mutants in a bacteriophage T4 mRNA processing site. Genes Dev., 6, 149-159 (1992).
25. Mudd, E. A., Prentki, P., Belin, D., and Krisch, H. M., Processing of unstable bacteriophage T4 gene 32 mRNAs into a stable species requires Escherichia coli ribonuclease E. EMBO J., 7, 3601-3607 (1988).
26. Patel, A. M. and Dunn, S. D., Degradation of Escherichia coli uncB mRNA by multiple endonucleolytic cleavages. J. Bacteriol., 177, 3917-3922 (1995).
27. Nilsson, P., Naureckiene, S., and Uhlin, B. E., Mutations affecting mRNA processing and fimbrial biogenesis in the Escherichia coli pap operon. J. Bacteriol., 178, 683-690 (1996).
28. Jiang, X., Diwa, A., and Belasco, J. G., Regions of RNase E important for 5?-end-dependent RNA cleavage and autoregulated synthesis. J. Bacteriol., 182, 2468-2475 (2000).
29. Gilbert, M., Watson, D. C., Cunningham, A. M., Jennings, M. P., Young, N. M., and Wakarchuk, W. W., Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae. J. Biol. Chem, 271, 28271-28276 (1996).
30. Leyland, M. L. and Kelly, D., Purification and characterization of a monomeric isocitrate dehydrogenase with dual coenzyme specificity from the photosynthetic bacterium, Rhodomicrobium vannie-lii. Eur. J. Biochem., 202, 85-93 (1991).