Regulation of a NAD+Kinase Activity Isolated from Asynchronous Cultures of the Achlorophyllous ZC Mutant of Euglena gracilis

Zeitschrift fur Naturforschung - Section C Journal of Biosciences

Volumn 52, Issue 9-10, 1997, Pages 623-635

  Crescenzoa, Marie Anne Pou de ^a   Laval Martina, Danielle L ^a   Goto, Ken ^b   Carré, Isabelle A ^c  

^a UNIVERSITÉ D'ANGERS   (France)

^b OBIHIRO UNIVERSITY OF AGRICULTURE AND VETERINARY MEDICINE   (Japan)

^c UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EUGLENA GRACILIS;

EID: 0031238955     PISSN: 09395075     EISSN: None     Source Type: Journal    
DOI: 10.1515/znc-1997-9-1009     Document Type: Article

References (37)

1. Afanasieva T. P., Filippovich S. Y., Sokolovsky V. Y. and Kritsky M. S. (1982), Developmental regulation of NAD kinase (EC 2.7.1.23) in Arch. Microbiol. 133 (4), 307-311.
2. Allan E. and Trewavas, A. (1985). Quantitative changes in calmodulin and NAD kinase during early cell development in the root apex of Pisum sativum L. Planta 165, 493-501.
3. +kinase. Eur. J. Biochem. 5, 444-450.
4. Apps D. K. (1970), The NAD kinases of Saccharomyces cerevisiae. Eur. J. Biochem. 13, 223-230.
5. Apps D. K. (1971). Inhibition of pigeon liver NAD kinase by a non-phosphorylatible analogue of NAD. FEBS Lett. 15 (4), 277-280.
6. +kinase. The structural and kinetic basis of the regulation by NADPH. Eur. J. Biochem. 55, 475-483.
7. Babu Y. S., Sack J. S., Greenhough T. J., Bugg C. E., Means A. R. and Cook, W. J. (1985), Three-dimensional structure of calmodulin. Nature 315, 37-40.
8. Bradford M. (1976), A rapid and sensitive method for the quantification of microgram quantities of proteins utilizine; the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
9. Bulygina E. R. and Telepneva V. I. (1982), Properties of pigeon heart nicotinamide adenine dinucleotide kinase. Biochem. Int. 4 (2). 135-141.
10. +kinase: purification, properties and affinity gel studies. Int. J. Biochem. 14, 839-844.
11. Calvayrac R. and Ledoigt G. (1976), Development of Euglena in presence of DCMU: evolution of the plas- tidome depending on the tension of oxygen. Plant Sci. Lett. 7, 249-263.
12. Carre I. A., Oster A. S. Laval-Martin D. L. and Edmunds, L. N. Jr. (1989), Entrainment and phase-shifting of the circadian rhythm of cell division by light in cultures of the achlorophyllous ZC mutant of Euglena gracilis. Curr. Microbiol. 19, 223-229.
13. Cheng W. and Roth J. R. (1994), Evidence for two NAD kinases in Salmonella typhimurium. J. Bacteriol. 176, 4260-4268.
14. +kinase from Azotobacter vinelandii and rabbit liver. Methods Enzymol. XVIIB. 149-156.
15. 2+-calmodulin dependent NAD kinase from corn is located in the outer mitochondrial membrane. J. Biol. Chem. 259, 184-189.
16. Edmunds L. N. Jr. (1988), Cellular and Molecular Bases of Biological Clocks. Springer-Verlag. New York.
17. Edmunds L. N. Jr. and Funch R. R. (1969), Effects of ‘skeleton’ photoperiods and high frequency light-dark cycles on the rhythm of cell division in synchronized cultures of Euglena. Planta. 87, 134-163.
18. Enander K. and Rydström J. (1982), Energy-linked nicotinamide nucleotide transhydrogenase: kinetics and regulation of purified and reconstituted transhydrogenase from beef heart mitochondria. J. Biol. Chem. 257 (24), 14760-14766.
19. +kinase in the silkworm. Bombyx mori L. Insect. Biochem., 20 (2), 99-104.
20. Goto K. (1984), Causal relationships among metabolic circadian rhythms in Lemna. Z. Naturforsch. C 39, 73-84.
21. Goto K., Laval-Martin D. L. and Edmunds L. N. Jr., (1985), Biochemical modeling of an autonomously oscillatory circadian clock in Euglena. Science. 228, 1284-1288.
22. Henderson P. J. F. (1986), Statistical analysis of enzyme kinetic data. In: Enzyme Assays, a Practical Approach (Eisenthal, R. and Danson, M. J., ed.). Oxford University Press, 277-316.
23. Iwahashi Y., Hitoshio A., Tajima N. and Nakamura T., (1989), Characterisation of NADH kinase from Saccharomices cerevisae. J. Biochem. 105, 588-593.
24. Laval-Martin D. L., Carré, I. A., Barbera S. J. and Edmunds L. N., Jr. (1990a), Rhythmic changes in the activities of NAD kinase and NADP phosphatase in the achlorophyllous ZC mutant of Euglena gracilis Klebs. Arch. Biochem. Biophys. 276, 433-441.
25. +. in dividing and non dividing cells of achlorophyllous ZC mutant of Euglena gracilis Klebs. Chronobiol. Int. 7, 99-105.
26. Marmé, D. (1985), The role of calcium in the cellular regulation of plant metabolism. Physiol. Veg. 23 (5): 945-953.
27. Marmé, D. and Dieter P. (1983), Calcium and Cell Function (Cheung., W. Y., ed). Academic Press, New York, Vol IV, pp. 263-311.
28. +kinase-A review. Int. J. Biochem, Vol. 17, 1-11.
29. Muto S. and Miyachi S. (1986), Molecular and Cellular Aspects of Calcium in Plant Development (Trewavas, A. J., ed.). Plenum PubI. New York, London, pp. 107-114.
30. Oka H. and Field J. B. (1968), Inhibition of rat liver nicotinamide adenine dinucleotide kinase by reduced nicotinamide adenine. J. Biol. Chem. 243, 815-819.
31. Roberts D. M., Lukas T. J. and Watterson D. M. (1985), Critical Review. Plant Science 4, 311-339.
32. 2+, calmodulin-independent activity in the stroma of pea chloroplasts. FEBS Lett. 197, 332-338.
33. Slaski J. J. (1989), Effect of aluminium on calmodulin- dependent and calmodulin-independent NAD kinase activity in wheat (Triticum aestivum L.) root tips. J. Plant Physiol. 133, 696-701.
34. Telepneva V. I. and Insarova I. D. (1976), Study of the quaternary structure of NAD kinase of rabbit skeletal muscles. Dokl. Akad. Nauk SSSR 218, 234-237.
35. Thompson-Amann B., Mulqueen P. and Horrocks W., Jr. (1992), A continuous spectrophotometric assay for the activation of plant NAD kinase by calmodulin, calcium(II), and europium(III) ions. J. Biochem. Biophys. Meth. 25, 207-217.
36. Tseng Y. M., Harris B. G. and Jacobson M. K. (1979), Isolation and characterisation of yeast nicotinamide adenine dinucleotide kinase. Biochem. Biophys. Acta. 568, 205-214.
37. +kinase and changes in nicotinamide coenzyme levels in lettuce half-seeds caused by red light. J. Plant Physiol. 143, 693-698.