Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Potential-dependent anion transport across tonoplast vesicles from oat roots

Conference · · Plant Physiol., Suppl.; (United States)
OSTI ID:5017983

Potential-dependent anion movement was monitored as dissipation of membrane potentials using the fluorescence probe Oxonol V. The potentials (positive inside) were generated with the H/sup +/-pumping pyrophosphatase (PPase) associated with tonoplast vesicles. Unlike the H/sup +/-ATPase, the PPase is stimulated by K/sup +/ and insensitive to anions. The order of permeability for the anions tested was: SCN/sup -/ > Cl/sup -/ = NO/sub 3//sup -/ > Br/sup -/ >> SO/sub 4//sup =/ = H/sub 2/PO/sub 4//sup -/ > acetate = malate > iminodiacetate. Kinetic studies showed that the Cl/sup -/ and NO/sub 3//sup -/ transport activities are saturable (Km = 2 and 5 mM), indicating the existence of proteinaceous anion channels. In contrast to the H/sup +//Cl/sup -/ symporter identified in the same vesicles, the potential-dependent Cl/sup -/ transport was insensitive to 4,4'-diisothiocyano-2,2'-stilbene disulfonic acid. These results suggest the existence of at least two different mechanisms for Cl/sup -/ transport in these vesicles. The potentials generated by the H/sup +/-ATPase and the H/sup +/-PPase were non-additive, giving further support to the notion that both enzymes are on the same population of vesicles.

Research Organization:
Univ. of Maryland, College Park
OSTI ID:
5017983
Journal Information:
Plant Physiol., Suppl.; (United States), Journal Name: Plant Physiol., Suppl.; (United States) Vol. 80:4; ISSN PPYSA
Country of Publication:
United States
Language:
English