Biologia plantarum 46:195-202, 2003 | DOI: 10.1023/B:BIOP.0000022251.40891.ae

Nucleotide-Dependent Isomerization of Glutamate Dehydrogenase in Relation to Total RNA Contents of Peanut

G.O. Osuji1, W.C. Madu1, C. Braithwaite1, A. Beyene1, P.S. Roberts1, A. Bulgin1, V. Wright1
1 Cooperative Agricultural Research Center, Prairie View A&M University, Prairie View, USA

The physiological function of glutamate dehydrogenase (GDH) was investigated by treating germinating peanut (Arachis hypogaea L.) seeds with nucleoside triphosphate (NTP) solutions in order to alter the isoenzyme distribution patterns. The free nucleosides and nucleotides of the GTP-treated peanut were the highest [8.7 μmol g-1(f.m.)], and they decreased through the ATP-treated peanut [5.8 μmol g-1(f.m.)], and CTP-treated peanut [5.5 μmol g-1(f.m.)], to the UTP-treated peanut [4.1 μmol g-1(f.m.)]. The combination of 4 NTPs induced 20 % higher content of Pi [173 nmol g-1(f.m.)] than in the control, but the combined ATP+UTP treatment induced the lowest (93.0 nmol g-1(f.m.)] Pi. The 4 NTP treatment also induced the highest number of GDH isoenzymes (28) followed by the purine NTP treatments (15 to 20), but the pyrimidine NTP treatments and the combined purine + pyrimidine NTP treatments induced the lowest numbers (<15) of isoenzymes. The deamination/amination ratios were generally higher in the UTP (0.11), and CTP (0.06) treated peanuts than in the GTP (0.04), and ATP (0.07) treated peanuts. There were mutual relationships between higher numbers of GDH isoenzymes present in the GTP-, and ATP-treated peanuts and higher RNA (236.5 and 239.4 μg g-1, respectively) contents on one hand, and between the lower numbers of isoenzymes in the CTP-, and UTP-treated peanuts and lower RNA (162.0 and 152.5 μg g-1, respectively) contents. The recurrent relationships of the effects of the NTP treatments of peanut were UTP > ATP > CTP > GTP.

Keywords: Arachis hypogaea; chromatography; deamination, amination ratio; free nucleotides; inorganic phosphate
Subjects: Arachis hypogaea; deamination/amination ratio; germination; glutamate dehydrogenase; nucleoside triphosphate, seed germination; nucleotide-dependent isomerization od GDH; peanut, RNA content

Published: September 1, 2003Show citation

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Osuji, G.O., Madu, W.C., Braithwaite, C., Beyene, A., Roberts, P.S., Bulgin, A., & Wright, V. (2003). Nucleotide-Dependent Isomerization of Glutamate Dehydrogenase in Relation to Total RNA Contents of Peanut. Biologia plantarum, 46(2), 195-202. doi: 10.1023/B:BIOP.0000022251.40891.ae.
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    References

    1. Ameziane, R., Bernhard, K., Lightfoot, D.: Expression of bacterial gdhA gene encoding a NADPH glutamate dehydrogenase in tobacco affects plant growth and development.-Plant Soil 221: 47-57, 2000. Go to original source...
    2. Aubert, S., Bligny, R., Douce, R., Gout, E., Ratcliffe, R.G., Roberts, J.K.M.: Contribution of glutamate dehydrogenase to mitochondrial glutamate metabolism studied by 13C and 31P magnetic resonance.-J. exp. Bot. 52: 37-45, 2001. Go to original source...
    3. Blackwell, R.D., Murray, A.J.S., Lea, P.J.: Enzymes of the photorespiratory carbon pathway.-In: Lea, P.J. (ed.): Methods in Plant Biochemistry. Pp. 129-144. Academic Press, New York 1990. Go to original source...
    4. Brown, E.G.: Nucleic acids and their derivatives in the control of development.-In: Farkas, G.L. (ed.): Nucleic Acids and Proteins in Higher Plants. Pp. 337-343. Akadémiai Kiadó, Budapest 1972.
    5. Cammaerts, D., Jacobs, M.: A study of the polymorphism and the genetic control of the glutamate dehydrogenase isozymes in Arabidopsis thaliana.-Plant Sci. Lett. 31: 65-73, 1983. Go to original source...
    6. Clarkson, D.T., Scattergood, C.B.: Growth and phosphate transport in barley and tomato plants during the development of, and recovery from phosphate-stress.-J. exp. Bot. 33: 865-875, 1982. Go to original source...
    7. Coruzzi, G., Bush, D.R.: Nitrogen and carbon nutrient and metabolite signaling in plants.-Plant Physiol. 125: 61-64, 2001. Go to original source...
    8. Coruzzi, G. M., Zhou, L.: Carbon and nitrogen sensing and signaling in plants: emerging matrix effects.-Curr. Opinion Plant Biol. 4: 247-253, 2001.
    9. Grierson, D., Slater, A., Speirs, J., Tucker, G.A.: The appearance of polygalacturonase mRNA in tomatoes.-Planta 163: 263-271, 1985. Go to original source...
    10. Harden, T.K., Boyer, J.L., Dougherty, R.W.: Drug analysis based on signaling responses to G-protein-coupled receptors.-J. Receptor Signal Transduct. 21: 167-190, 2001. Go to original source...
    11. Henderson, J.F., Paterson, A.R.P.: Nucleotide Metabolism.-Academic Press, New York 1973.
    12. Kakie, T.: Phosphorus fractions in tobacco plants as affected by phosphate application.-Soil Sci. Plant Nutr. 15: 81-85, 1969. Go to original source...
    13. Lea, P.J., Blackwell, R.D., Joy, K.W.: Ammonia assimilation in higher plants.-In: Mengel, K., Pilbeam, D.J. (ed.): Nitrogen Metabolism of Plants. Pp. 153-186. Clarendon Press, Oxford 1992.
    14. Leon, E., De La Haba, P., Maldonado, J.M.: Changes in the levels of enzymes involved in ammonia assimilation during the development of Phaseolus vulgaris seedlings. Effects of exogenous ammonia.-Physiol. Plant. 80: 20-26, 1990. Go to original source...
    15. Lettgen, W., Britsch, L., Kasemir, H.: The effects of light and exogenously supplied ammonium ions on glutamate dehydrogenase activity and isoforms in young mustard (Sinapis alba L.) seedlings.-Bot. Acta 102: 189-195, 1989. Go to original source...
    16. Lightfoot, D.A., Long, L., Vidal, M.E.: Plants containing bacterial gdhA and methods of their use thereof.-US patent # 5,998,700, 1999.
    17. Lollier, M., Jaquet, L., Nedeva, T., Lacroute, F., Potier, S., Souciet, J.L.: As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe.-Curr. Genet. 28: 138-149, 1995. Go to original source...
    18. Loulakakis, K.A., Roubelakis-Angelakis, K.A.: Plant NAD(H)-glutamate dehydrogenase consists of two subunit polypeptides and their participation in the seven isoenzymes occurs in an ordered ratio.-Plant Physiol. 97: 104-111, 1991. Go to original source...
    19. Loyola-Vargas, V.M., De Jimenez, E.S.: Differential role of glutamate dehydrogenase in nitrogen metabolism of maize tissues.-Plant Physiol. 76: 536-540, 1984. Go to original source...
    20. Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J.: Protein measurement with the Folin phenol reagent.-J. biol. Chem. 193: 265-275, 1951.
    21. Nauen, W., Hartmann, T.: Glutamate dehydrogenase from Pisum sativum L.-Planta 148: 7-16, 1980. Go to original source...
    22. Osuji, G.O.: Peanut glutamate dehydrogenase: A target site of herbicide action.-In: Ando, T., Fujita, K., Mea, T., Matsumoto, H., Mori, S., Sekiya, J. (ed.): Plant Nutrition for Sustainable Food Production and Environment. Pp. 845-850. Kluwer Academic Publishers, Dordrecht-Boston-London 1997. Go to original source...
    23. Osuji, G.O., Braithwaite, C.: Signaling by glutamate dehydrogenase in response to pesticide treatment and nitrogen fertilization of peanut (Arachis hypogaea L.).-J. Agr. Food Chem. 47: 3332-3344. 1999. Go to original source...
    24. Osuji, G.O., Braithwaite, C., Fordjour, K., Madu, W., Beyene, A., Roberts, P.S., Wright, V.: Purification of glutamate dehydrogenase isoenzymes and characterization of their substrate specificities.-Prep. Biochem. Biotech. 33: 13-28, 2002b.
    25. Osuji, G.O., Braithwaite, C., Pointer, R., Reyes, J.: Pesticide inactivation of peanut GDH: Biochemical basis of the enzyme's isomerization.-J. agr. Food Chem. 47: 3345-3351, 1999. Go to original source...
    26. Osuji, G.O., Haby, V.A., Beyene, A., Madu, W.C., Mangaroo, A.S.: The isomerization of glutamate dehydrogenase in response to lead toxicity in maize.-Biol. Plant. 40: 389-398, 1997/98. Go to original source...
    27. Osuji, G.O., Madu, W.C.: Ammonium ion-dependent isomerization of glutamate dehydrogenase in relation to glutamate synthesis in maize.-Phytochemistry 39: 495-503, 1995. Go to original source...
    28. Osuji, G.O., Madu, W.C.: Ammonium ion salvage by glutamate dehydrogenase during defence response in maize.-Phytochemistry 42: 1491-1498, 1996.
    29. Osuji, G.O., Madu, W.C.: Regulation of peanut glutamate dehydrogenase by methionine sulphoximine.-Phytochemistry 46: 817-825, 1997a. Go to original source...
    30. Osuji, G.O., Madu, W.C.: Regulation of sweet potato growth and differentiation by glutamate dehydrogenase.-Can. J. Bot. 75: 1070-1078, 1997b.
    31. Osuji, G.O., Madu, W.C., Braithwaite, C., Beyene, A., Roberts, P.S., Bulgin, A., Wright, V.: Biomass enhancement in maize and soybean in response to glutamate dehydrogenase isomerization.-Biol. Plant. 47: 45-52, 2003a.
    32. Osuji, G.O., Mangaroo, A.S., Roberts, P.S.: In vitro isomerization of glutamate dehydrogenase in relation to phytosequesteration of lead.-SAAS Bull. Biochem. Biotech. 14: 60-72, 2001.
    33. Osuji, G.O., Ory, R.L.: Regulation of allantoin and allantoic acid degradation in the yam and sweet potato.-J. agr. Food Chem. 35: 219-223, 1987. Go to original source...
    34. Osuji, G.O., Ory, R.L.: Purine degradative pathway of the yam and sweet potato.-J. agr. Food Chem. 34: 599-602, 1986. Go to original source...
    35. Osuji, G.O., Reyes, J.C., Mangaroo, A.S.: Glutamate dehydrogenase isomerization: A simple method for diagnosing nitrogen, phosphorus, and potassium sufficiency in maize (Zea mays L.).-J. agr. Food Chem. 46: 2395-2401, 1998.
    36. Perbal, B.: A Practical Guide to Molecular Cloning.-John Wiley, New York 1988.
    37. Ratajczak, L., Ratajczak, W., Mazurowa, H.: The effects of carbon and nitrogen sources on the activity of glutamine synthetase and glutamate dehydrogenase in lupine embryonic axes.-Physiol. Plant. 51: 277-280, 1981. Go to original source...
    38. Robinson, S.A., Slade, A.P., Fox, G.G., Phillips, R., Ratcliffe, G., Stewart, G.R.: The role of glutamate dehydrogenase in plant nitrogen metabolism.-Plant Physiol. 95: 509-516, 1990.
    39. Robinson, S.A., Stewart, G.R., Phillips, R.: Regulation of glutamate dehydrogenase activity in relation to carbon limitation and protein catabolism in carrot cell suspension cultures.-Plant Physiol. 98: 1190-1195, 1992. Go to original source...
    40. Segel, I.H.: Biochemical Calculations. 2nd Edition.-John Wiley, New York 1976
    41. Senecoff, J.F., McKinney, E.C., Meagher, R.B.: De novo purine synthesis in Arabidopsis thaliana.-Plant Physiol. 112: 905-917, 1996.
    42. Smith, P.M.C., Atkins, C.A.: Purine biosynthesis. Big in cell division, even bigger in nitrogen assimilation.-Plant Physiol. 128: 793-802, 2002. Go to original source...
    43. Stewart, G.R., Shatilov, V.R., Turnbull, M.H., Robinson, S.A., Goodall, R.: Evidence that glutamate dehydrogenase plays a role in the oxidative deamination of glutamate in seedlings of Zea mays.-Aust. J. Plant Physiol. 22: 805-809. 1995. Go to original source...
    44. Srivastava, H.S., Singh, R.P.: Role and regulation of L-glutamate dehydrogenase activity in higher plants.-Phytochemistry 26: 597-610, 1987. Go to original source...
    45. Wasternack, C.: Degradation of pyrimidines-enzymes, localization and role in metabolism.-Biochem. Physiol. Pflanz. 173: 467-499, 1978. Go to original source...
    46. Watanabe, M., Nakayama, H., Watanabe, Y., Shimada, N.: Induction of a specific isoenzyme of glutamate dehydrogenase during isolation and the first 48 h of culture of Brassica napus leaf protoplasts.-Physiol. Plant. 86: 231-235, 1992. Go to original source...
    47. Zink, M. Regulation of ammonium-assimilating enzymes by various nitrogen sources in cultured Ipomoea spp.-Can. J. Bot. 67: 3137-3133, 1989. Go to original source...

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