Abstract
Discontinuous sucrose gradient fractionations indicate that the high-affinity auxin binding protein which can be solubilized from the microsomes of coleoptiles and primary leaves of Zea mays L. seedlings is probably located in the endoplasmic reticulum (ER). Since aromatic hydroxylations are enzymatic activities typical of the ER of plant cells, we have examined the effects of several electron-transport inhibitors on the binding of 1-naphthylacetic acid (NAA). NaN3 strongly inhibits this binding, but KCN and CO do not. Trans-cinnamic acid and trans-p-coumaric acid, which are the substrates of ER hydroxylase activities in plants (but which are themselves not auxins), also inhibit this binding. Supernatant fractions from corn shoots contain factors inhibitory to the binding of NAA to the intact membranes and solubilized Site I auxin-binding protein. Here we show that these factors are competitive inhibitors of the binding of [14C]NAA but do not change the apparent affinity of the protein for indoleacetic acid, 2,4-dichlorophenoxyacetic acid or naphthoxyacetic acid. Several tissues were assayed for factors inhibitory to auxin binding to the solubilized protein, but only supernants from corn shoots were markedly inhibitory at low concentrations.
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Abbreviations
- 2,4-D:
-
2,4-dichlorophenoxyacetic acid
- ER:
-
endoplasmic reticulum
- IAA:
-
3-indolylacetic acid
- nKP:
-
n x 100 x g pellet
- NAA:
-
1-naphthylacetic acid
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C.I.W.-D.P.B. Publication No. 656
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Cross, J.W., Briggs, W.R. Solubilized auxin-binding protein. Planta 146, 263–270 (1979). https://doi.org/10.1007/BF00387796
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DOI: https://doi.org/10.1007/BF00387796