Abstract
The attachment of glycolate oxidase to the peroxisomal fraction derived from etiolated barley leaves (Hordeum vulgare L. cr. Dvir) is affected by light. The effect of red irradiation is reversed by subsequent far-red irradiation, indicating the involvement of phytochrome. This phytochrome effect is assumed to be related to phytochrome binding. Indeed, prevention by filipin (1.2·10-6 mol g-1 f wt) or cholesterol of phytochrome binding to membranes abolishes the effect of light on the interaction between glycolate oxidase and the peroxisomal fraction. Glycolate oxidase binding is affected by addition of quasi-ionophores such as gramicidin and filipin at a concentration of 0.6·10-3 mol g-1 f wt. This fact indicates that peroxisome-glycolate oxidase interaction may be affected by membrane potential. Since both ion transport and membrane potential are known to be affected by phytochrome, it is proposed that phytochrome acts in the light-induced modulation of glycolate oxidase attachment as a quasi-ionophore.
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Abbreviations
- GO:
-
glycolate oxidase
- Pr and Pfr:
-
phytochrome forms absorbing in red and far-red, respectively
- R and F:
-
red and far-red irradiation
- Cumulative 20 Kp:
-
20,000 g pellet obtained by centrifugation of the crude extract
- 1 Kp:
-
1,000 g pellet
- 20 Kp:
-
20,000 g pellet, obtained by centrifugation of 1 Kp supernatant
- 1 Kp′, 20 Kp′ and cumulative 20 Kp′:
-
pellets obtained after density centrifugation through a sucrose cushion
References
Appelmans, F., Wattiaux, R., de Duve, C. (1955) Tissue fractionation studies. 5. The association of acid phosphatase with a special class of cytoplasmic granules in rat liver. Biochem. J. 59, 438–445
Brownlee, C., Kendrick, R.E. (1977) Phytochrome and potassium uptake by Mung bean hypocotyl section. Planta 137, 61–64
Brownlee, C., Roth-Bejerano, N., Kendrick, R.E. (1979) The molecular mode of phytochrome action. Sci. Progr. 66, 217–229
Fierabend, J., Beevers, H. (1972a) Developmental studies on microbodies in Wheat leaves. 1. Conditions influencing enzyme development. Plant Physiol. 49, 28–32
Fierabend, J., Beevers, H. (1972b) Developmental studies on microbodies in Wheat leaves. 2. Ontogeny of particulate enzyme association. Plant Physiol. 49, 33–39
Hampp, R., Schmidt, H.W. (1977) Regulation of membrane properties of mitochondria and plastids during development. 1. Action of phytochrome in situ. Z. Pflanzenphysiol. 82, 68–77
Haupt, W., Weisenseel, M.H. (1976) Physiological evidence and thoughts on localized responses, intracellular localization and action of phytochrome. In: Light and plant development, pp 63–74. Smith, H. ed. Butterworths, London
Hess, J.L., Tolbert, N.E. (1967) Glycolate pathway in algae. Plant Physiol. 42, 371–379
Jose, A.M. (1977) Phytochrome modulation of ATPase activity in membrane fraction from Phaseolus. Planta 137, 203–206
Jose, A.M., Schäfer, E. (1979) Red/far red modulation in vitro of enzyme activity in a membrane fraction of Phaseolus aureus. Planta 146, 75–81
Katchalsky, E., Silman, I., Goldman, R. (1971) Effect of the microenvironment on the mode of action of immobilized enzymes. Adv. Enzymol. 34, 445–556
Kimelberg, H.K., Lee, L.P. (1970) Interaction of cytochrome c with phospholipid membrane. 1. Binding of cytochrome c to phospholipid liquid crustal. J. Membr. Biol. 2, 235–251
De Kruijff, R., Demel, R.A. (1974) Polyene antibiotic-sterol interaction in membranes of Acholeplasma Laidlawii cells and lecitin liposomes. 3. Molecular structure of the polyene antibioticcholesterol complexes. Biochim. Biophys. Acta 339, 57–70
Lowry, O.H., Rosenborough, N.J., Farr, A.L., Randal, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 256–273
Löppert, H., Kronberger, W., Kandeler, R. (1978) Phytochromemediated changes in the membrane potential of subepidermal cells of Lemna paucicostata 6746. Planta 138, 133–136
Marmé, D. (1977) Phytochrome: Membranes as possible sites of primary action. Annu. Rev. Plant Physiol. 28, 173–198
Muñoz, E., Salton, M.R.J., Ng, M.H., Schor, M.T. (1969) Membrane adenosine triphosphate of Micrococcus Lysodikticus Purification, properties of the “soluble” enzyme and properties of the membrane bound enzyme. Eur. J. Biochem. 7, 490–501
Penel, C., Greppin, H., Boisard, J. (1976) In vitro photomodulation of a peroxidase activity through membrane-bound phytochrome. Plant Sci. Lett. 6, 117–121
Pratt, L.H. (1973) Molecular properties of phytochrome. Photochem. Photobiol. 27, 81–105
Pressman, B.C. (1976) Biological application of ionophores. Annu. Rev. Biochem. 45, 501–530
Racusen, R.H. (1976) Phytochrome control of electrical potential and intercellular coupling in oat-coleoptile tissue. Planta 132, 25–29
Roth-Bejerano, N., Lips, S.H. (1978) Binding of glycolate oxidase to peroxisomal membrane as affected by light. Photochem. Photobiol. 27, 171–175
Roth-Bejerano, N., Kendrick, R.E. (1979a) Phytochrome pelletability in Barley. Physiol. Plant. 97, 67–72
Roth-Bejerano, N., Kendrick, R.E. (1979b) Effect of filipin and steroids on phytochrome pelletability. Plant Physiol. 63, 503–506
Satter, R.L., Geballe, G.T., Galston, A.W. (1974) Potassium flux and leaf movement in Samanea saman 2. Phytochrome controlled movement. J. Gen. Physiol. 64, 431–442
Schmidt, H.W., Hampp, R. (1977) Regulation of membrane properties of mitochondria and plastids during chloroplast development in cell-free system. Z. Pflanzenphysiol. 5, 428–434
Schopfer, P., Bajracharya, D., Bergfeld, R., Falk, H. (1976) Phytochrome-mediated transformation of glyoxysomes into peroxisomes in the cotyledons of mustard (Sinapis alba L.) seedlings. Planta 133, 73–80
Tanada, T.A. (1968) A rapid photoconversible response of barley root tips in presence of 3-indolacetic acid. Proc Natl. Acad. Sci. USA 59, 376–380
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Roth-Bejerano, N. Nature of the phytochrome effect on the binding of glycolate oxidase to peroxisomes in vitro. Planta 149, 252–256 (1980). https://doi.org/10.1007/BF00384561
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DOI: https://doi.org/10.1007/BF00384561