Abstract
Two types of auxin-binding sites (sites I and II) in membranes from maize (Zea mays L.) coleoptiles were characterized. Site I was a protein with a relative molecular mass of 21 000, and the distribution of site I protein on sucrose density gradient fractionation coincided with that of NADH-cytochrome-c reductase (EC 1.6.99.3), a marker enzyme of the endoplasmic reticulum. Immunoprecipitation and immunoblotting studies showed that the content of site I protein in maize coleoptiles was approx. 2 μg·(g FW)-1. Site II occurred in higher-density fractions and also differed immunologically from site I. Site I was present at the early developmental stage of the coleoptile and increased only twice during coleoptile growth between day 2 and 4. Site II activity was low at the early stage and increased more substantially between day 3 and 4, a period of rapid growth of the coleoptile. Both sites decreased concurrently after day 4, followed by a reduction in the growth rate of the coleoptile. Coleoptiles with the outer epidermis removed showed a lower site I activity than intact coleoptiles, indicating that site I was concentrated in the outer epidermis. Site II, in contrast, remained constant after removal of the outer epidermis. The results indicate that site I is not a precursor of site II and that the two sites are involved in different cellular functions.
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Abbreviations
- FW:
-
fresh weight
- M r :
-
relative molecular mass
- 1-NAA:
-
1-naphthaleneacetic acid
- 2-NAA:
-
2-naphthaleneacetic acid
- SDS-PAGE:
-
sodium dodecyl sulfate-polyacrylamide gel electrophoresis
References
Batt, S., Venis, M.A. (1976) Separation and localization of two classes of auxin binding sites in corn coleoptile membranes Planta 130, 15–21
Batt, S., Wilkins, M.B., Venis, M.A. (1976) Auxin binding to corn coleoptile membranes: kinetics and specificity. Planta 130, 7–13
Benning, C. (1986) Evidence supporting a model of voltagedependent uptake of auxin into Cucurbita vesicles. Planta 169, 228–237
Benovic, J.L., Shorr, R.G.L., Caron, M.G., Lefkowitz, R.J. (1984) The mammalian β2 receptor: purification and characterization. Biochemistry 23, 4510–4518
Buckhout, T.J., Young, K.A., Low, P.S., Morré, D.J. (1981) In vitro promotion by auxins of divalent ion release from soybean membranes. Plant Physiol. 68, 512–515
Cheng, S.-Y., Hasumura, S., Willingham, M.C., Pastan, I. (1986) Purification and characterization of a membraneassociated 3,3′,5-triiodo-L-thyronine binding protein from a human carcinoma cell line. Proc. Natl. Acad. Sci. USA 83, 947–951
Dohrmann, U., Hertel, R., Kowalik, H. (1978) Properties of auxin binding sites in different subcellular fractions from maize coleoptiles. Planta 140, 97–106
Gabathuler, R., Cleland, R.E. (1985) Auxin regulation of a proton translocating ATPase in pea root plasma membrane vesicles. Plant Physiol. 79, 1080–1085
Guilfoyle, T.J. (1986) Auxin-regulated gene expression in higher plants. CRC Crit. Rev. Plant Sci. 4, 247–276
Haga, K., Haga, T. (1985) Purification of the muscarinic acetylcholine receptor from porcine brain. J. Biol. Chem. 260, 7927–7935
Hertel, R. (1983) The mechanism of auxin transport as a model for auxin action. Z. Pflanzenphysiol. 112, 53–67
Hertel, R., Lomax, T.L., Briggs, W.R. (1983) Auxin transport in membrane vesicles from Cucurbita pepo L. Planta 157, 193–201
Hertel, R., Thomson, K.-St., Russo V.E.A. (1972) In-vitro auxin binding to particulate cell fractions from corn coleoptiles. Planta 107, 325–340
Heyn, A., Hoffmann, S., Hertel, R. (1987) In-vitro auxin transport in membrane vesicles from maize coleoptiles. Planta 172, 285–287
Jacobs, M., Hertel, R. (1978) Auxin binding to subcellular fractions from Cucurbita hypocotyls: in vitro evidence for an auxin transport carrier. Planta 142, 1–10
Key, J.L., Kroner, P., Walker, J., Hong, J.C., Ulrich, T.H., Ainley, W.M., Gantt, J.S., Nagao, R.T. (1986) Auxin-regulated gene expression. Phil. Trans. R. Soc. London Ser. B 314, 427–440
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685
Löbler, M., Klämbt, D. (1985) Auxin-binding protein from coleoptile membranes of corn (Zea mays L.). II. Localization of a putative auxin receptor. J. Biol. Chem. 260, 9854–9859
Lomax, T.L., Mehlhorn, R.J., Briggs, W.R. (1985) Active auxin uptake by zucchini membrane vesicles: quantitation using ESR volume and ΔpH determinations. PRoc. Natl. Acad. Sci. USA 82, 6541–6545
Lord, J.M., Kagawa, T., Moore, T.S., Beevers, H. (1973) Endoplasmic reticulum as the site of lecithin formation in castor bean endosperm. J. Cell. Biol. 57, 659–667
Morré, D.J., Gripshover, B., Monroe, A., Morré, J.T. (1984a) Phosphatidylinositol turnover in isolated soybean, membranes stimulated by the synthetic growth hormone 2,4-dichlorophenoxyacetic acid, J. Biol. Chem. 259, 15364–15368
Morré, D.J., Morré, J.T., Varnold, R.L. (1984b) Phosphorylation of membrane-located proteins of soybean in vitro and response to auxin. Plant Physiol. 75, 265–268
Morré, D.J., Navas, P., Penel, C., Castillo, F.J. (1986) Auxinstimulated NADH oxidase (semidehydroascorbate reductase) of soybean plasma membrane: role in acidification of cytoplasm? Protoplasma 133, 195–197
Murphy, G.J.P. (1980) A reassessment of the binding of naphthaleneacetic acid by membrane preparations from maize. Planta 149, 417–426
Ray, P.M., Dohrmann, U., Hertel, R. (1977a) Characterization of naphthaleneacetic acid binding to receptor sites on cellular membranes of maize coleoptile tissue. Plant Physiol. 59, 357–364
Ray, P.M., Dohrmann, U., Hertel, R. (1977b) Specificity of auxin-binding sites on maize coleoptile membranes as possible receptor sites for auxin action. Plant Physiol. 60, 585–591
Sabater, M., Rubery, P.H. (1987) Auxin carriers in Cucurbita vesicles. II. Evidence that carrier-mediated routes of both indole-3-acetic acid influx and efflux are electroimpelled. Planta 171, 507–513
Sakai, S. (1985) Auxin-binding protein in etiolated mung bean seedlings: purification and properties of auxin-binding protein-II. Plant Cell Physiol. 26, 184–192
Sakai, S., Hanagata, T. (1983) Purification of an auxin-binding protein from etiolated mung bean seedlings by affinity chromatography. Plant Cell Physiol. 24, 685–693
Sakai, S., Seki, J., Imaseki, H. (1986) Stimulation of RNA synthesis in isolated nuclei by auxin-binding proteins-I and-II. Plant Cell Physiol. 27, 635–643
Schneider, W.C. (1957) Determination of nucleic acids in tissues by pentose analysis. Methods Enzymol. 3, 680–684
Shimomura, S., Sotobayashi, T., Futai, M., Fukui, T. (1986) Purification and properties of an auxin-binding protein from maize shoot membranes. J. Biochem. 99, 1513–1524
Siegel, T.W., Ganguly, S., Jacobs, S., Rosen, O.M., Rubin, C.S. (1981) Purification and properties of the human placental insulin receptor. J. Biol. Chem. 256, 9266–9273
Theologis, A. (1986) Rapid gene regulation by auxin. Annu. Rev. Plant Physiol. 37, 407–438
Towbin, H., Staehelin, T., Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350–4354
van der Linde, P.C.G., Bouman, H., Mennes, A.M., Libbenga, K.R. (1984) A soluble auxin-binding protein from cultured tobacco tissues stimulates RNA synthesis in vitro. Planta 160, 102–108
Venis, M.A., Watson, P.J. (1978) Naturally occuring modifiers of auxin-receptor interaction in corn: identification as benzoxazolinones. Planta 142, 103–107
Vreugdenhil, D., Burgers, A., Libbenga, K.R. (1979) A particlebound auxin receptor from tobacco pith callus. Plant Sci. Lett. 16, 115–121
Walton, J.D., Ray, P.M. (1981) Evidence for receptor function of auxin binding sites in maize. Red light inhibition of mesocotyl elongation and auxin binding. Plant Physiol. 68, 1334–1338
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Shimomura, S., Inohara, N., Fukui, T. et al. Different properties of two types of auxin-binding sites in membranes from maize coleoptiles. Planta 175, 558–566 (1988). https://doi.org/10.1007/BF00393079
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DOI: https://doi.org/10.1007/BF00393079