Partial characterization of fusicoccin binding to receptor sites on oat root membranes
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-bonding 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/sup +//K/sup +/. pumps in FC-stimulated acidification and K/sup +/ uptake.
- Research Organization:
- Univ. of Washington, Seattle
- DOE Contract Number:
- EY-76-S-06-2225
- OSTI ID:
- 7080001
- Journal Information:
- Plant Physiol.; (United States), Journal Name: Plant Physiol.; (United States) Vol. 66:3; ISSN PLPHA
- Country of Publication:
- United States
- Language:
- English
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59 BASIC BIOLOGICAL SCIENCES
ALKALI METALS
ANTIGENS
ATP-ASE
BIOCHEMICAL REACTION KINETICS
BIOCHEMISTRY
BIOLOGY
BOTANY
CELL CONSTITUENTS
CELL CULTURES
CELL MEMBRANES
CEREALS
CHEMISTRY
CHROMATOGRAPHY
ELEMENTS
ENZYME ACTIVITY
ENZYMES
ESTERASES
FRACTIONATION
GRAMINEAE
GRASS
HYDROGEN
HYDROLASES
IN VITRO
ION EXCHANGE MATERIALS
KINETICS
MATERIALS
MEMBRANE TRANSPORT
MEMBRANES
METABOLISM
METALS
MOLECULAR STRUCTURE
NONMETALS
OATS
PHOSPHATASES
PLANT CELLS
PLANT TISSUES
PLANTS
POTASSIUM
REACTION KINETICS
ROOTS
SEPARATION PROCESSES
TEMPERATURE EFFECTS
TOXIC MATERIALS
TOXINS
UPTAKE