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Purification and identification of the fusicoccin binding protein from oat root plasma membraneFusicoccin (FC), a fungal phytotoxin, stimulates the H(+) -ATPase located in the plasma membrane (PM) of higher plants. The first event in the reaction chain leading to enhanced H(+) -efflux seems to be the binding of FC to a FC-binding protein (FCBP) in the PM. We solubilized 90% of the FCBP from oat (Avena sativa L. cv Victory) root PM in an active form with 1% octyl-glucoside. The FCBP was stabilized by the presence of protease inhibitors. The FCBP was purified by affinity chromatography using FC-linked adipic acid dihydrazide agarose (FC-AADA). Upon elution with 8 molar urea, two major protein bands on sodium dodecyl sulfate-polyaerylamide gel electrophoresis with molecular weights of 29,700 and 31,000 were obtained. Successive chromatography on BBAB Bio-Gel A, hexyl agarose, and FC-AADA resulted in the same two bands when the FC-AADA was eluted with sodium dodecyl sulfate. A direct correlation was made between 3H-FC-binding activity and the presence of the two protein bands. The stoichiometry of the 29,700 and 31,000 molecular weight bands was 1:2. This suggests that the FCBP occurs in the native form as a heterotrimer with an apparent molecular weight of approximately 92,000.
Document ID
Document Type
Reprint (Version printed in journal)
de Boer, A. H.
(University of Washington, Department of Botany Seattle 98195, United States)
Watson, B. A.
Cleland, R. E.
Date Acquired
August 21, 2013
Publication Date
January 1, 1989
Publication Information
Publication: Plant physiology
Volume: 89
ISSN: 0032-0889
Subject Category
Life Sciences (General)
Funding Number(s)
Distribution Limits
NASA Discipline Number 29-20
NASA Discipline Plant Biology
NASA Program Space Biology
Non-NASA Center

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