Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1974 May;53(5):717–722. doi: 10.1104/pp.53.5.717

Kinetics of Activation of Nicotinamide Adenine Dinucleotide Kinase by Phytochrome—Far Red-absorbing Form

Takafumi Tezuka a, Yukio Yamamoto b,1
PMCID: PMC541432  PMID: 16658776

Abstract

The effects of exogenous redox cofactors and purine analogues on the activation of the NAD kinase by Pfr were examined. Addition of phenazine methosulfate, flavin mononucleotide, or methylene blue increased the activation of NAD kinase by red light in a partially purified preparation of phytochrome. Phenazine methosulfate and flavin mononucleotide do not absorb light in the red or far red region, so they do not act as light receptors in this activation. Thus they probably intervene in electron transfer between phytochrome and NAD kinase. Addition of kinetin with these compounds increased photopotentiation further. In the presence of phenazine methosulfate and kinetin, the activation of NAD kinase by red light was counteracted by illumination with far red light immediately after red light.

The relation between the dose of illumination with red light and the degree of activation of NAD kinase was measured. Illumination for 5 minutes with 800 ergs cm−2 sec−1 of red light was sufficient to obtain maximal activation. In the dark, the activated state of NAD kinase was maintained for about 10 min and then rapidly lost. The time of preservation of the activated state was greatly shortened by illumination with far red light, indicating the participation of phytochrome.

Full text

PDF
717

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. HENDRICKS S. B. Metabolic control of timing. Science. 1963 Jul 5;141(3575):21–27. doi: 10.1126/science.141.3575.21. [DOI] [PubMed] [Google Scholar]
  2. HIRATA M., TOKUSHIGE M., INAGAKI A., HAYAISHI O. NUCLEOTIDE ACTIVATION OF THREONINE DEAMINASE FROM ESCHERICHIA COLI. J Biol Chem. 1965 Apr;240:1711–1717. [PubMed] [Google Scholar]
  3. HOCH G., MARTIN I. Photo-potentiation of adenosine triphosphate hydrolysis. Biochem Biophys Res Commun. 1963 Jul 26;12:223–228. doi: 10.1016/0006-291x(63)90194-3. [DOI] [PubMed] [Google Scholar]
  4. Hatch M. D., Slack C. R. Studies on the mechanism of activation and inactivation of pyruvate, phosphate dikinase. A possible regulatory role for the enzyme in the C4 dicarboxylic acid pathway of photosynthesis. Biochem J. 1969 May;112(5):549–558. doi: 10.1042/bj1120549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Jaffe M. J. Phytochrome-mediated bioelectric potentials in mung bean seedlings. Science. 1968 Nov 29;162(3857):1016–1017. doi: 10.1126/science.162.3857.1016. [DOI] [PubMed] [Google Scholar]
  6. KENT A. B., KREBS E. G., FISCHER E. H. Properties of crystalline phosphorylase b. J Biol Chem. 1958 May;232(1):549–558. [PubMed] [Google Scholar]
  7. Miller C. O. Similarity of Some Kinetin and Red Light Effects. Plant Physiol. 1956 Jul;31(4):318–319. doi: 10.1104/pp.31.4.318. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Miller C. O. The Relationship of the Kinetin and Red-Light Promotions of Lettuce Seed Germination. Plant Physiol. 1958 Mar;33(2):115–117. doi: 10.1104/pp.33.2.115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Miyamoto E., Kuo J. F., Greengard P. Cyclic nucleotide-dependent protein kinases. 3. Purification and properties of adenosine 3',5'-monophosphate-dependent protein kinase from bovine brain. J Biol Chem. 1969 Dec 10;244(23):6395–6402. [PubMed] [Google Scholar]
  10. NEUMANN J., JAGENDORF A. T. LIGHT-INDUCED PH CHANGES RELATED PHOSPHORYLATION BY CHLOROPLASTS. Arch Biochem Biophys. 1964 Jul;107:109–119. doi: 10.1016/0003-9861(64)90276-0. [DOI] [PubMed] [Google Scholar]
  11. Newman I. A., Briggs W. R. Phytochrome-mediated Electric Potential Changes in Oat Seedlings. Plant Physiol. 1972 Dec;50(6):687–693. doi: 10.1104/pp.50.6.687. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Slack C. R. The photoactivation of a phosphopyruvate synthase in leaves of Amaranthus palmeri. Biochem Biophys Res Commun. 1968 Mar 12;30(5):483–488. doi: 10.1016/0006-291x(68)90077-6. [DOI] [PubMed] [Google Scholar]
  13. Tezuka T., Yamamoto Y. Photoregulation of Nicotinamide Adenine Dinucleotide Kinase Activity in Cell-free Extracts. Plant Physiol. 1972 Oct;50(4):458–462. doi: 10.1104/pp.50.4.458. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Yamamoto Y. NAD Kinase in Higher Plants. Plant Physiol. 1966 Mar;41(3):523–528. doi: 10.1104/pp.41.3.523. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Yamamoto Y. Pyridine Nucleotide Content in the Higher Plant. Effect of Age of Tissue. Plant Physiol. 1963 Jan;38(1):45–54. doi: 10.1104/pp.38.1.45. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Yamamoto Y. [Role of nicotinamide adenine dinucleotide phosphate in the regulation of metabolism in plants]. Seikagaku. 1970 Jan;42(1):1–18. [PubMed] [Google Scholar]
  17. Yamashita T., Butler W. L. Inhibition of the Hill Reaction by Tris and Restoration by Electron Donation to Photosystem II. Plant Physiol. 1969 Mar;44(3):435–438. doi: 10.1104/pp.44.3.435. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES