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. 1980 Sep;66(3):353–359. doi: 10.1104/pp.66.3.353

Partial Characterization of Fusicoccin Binding to Receptor Sites on Oat Root Membranes 1

Richard G Stout 1,2, Robert E Cleland 1
PMCID: PMC440633  PMID: 16661436

Abstract

The possibility that fusicoccin (FC) binds to plasma membrane-associated ATPases of oat (cv. Victory) roots has been examined. Specific FC-binding in vitro is localized primarily on plasma membrane-enriched fractions. This FC-binding is greatly reduced by pretreatment of the membrane vesicles at temperatures above 45 C or with trypsin, and the same treatments cause the release of already bound FC. These results support the idea that the FC receptor is a protein located on the plasma membrane.

Both active ATPases and FC-binding proteins were solubilized using 1% Triton X-100. When this material was fractionated using gel chromatography, the ATPase activity could be separated from the FC-binding proteins. The identity of the FC-binding proteins is discussed with regard to the extensive evidence which supports the involvement of plasma membrane-ATPase H+/K+ pumps in FC-stimulated acidification and K+ uptake.

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Selected References

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

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