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Vacuolar H(+)-ATPases: intra- and intermolecular interactions
Authors:Huss Markus  Vitavska Olga  Albertmelcher Andrea  Bockelmann Svenja  Nardmann Christin  Tabke Katharina  Tiburcy Felix  Wieczorek Helmut
Affiliation:University of Osnabrück, Faculty of Biology and Chemistry, Department of Animal Physiology, Barbarastrasse 11, 49076 Osnabrück, Germany. huss@biologie.uni-osnabrueck.de
Abstract:V-ATPases in eukaryotes are heteromultimeric, H(+)-transporting proteins. They are localized in a multitude of different membranes and energize many different transport processes. Unique features of V-ATPases are, on the one hand, their ability to regulate enzymatic and ion transporting activity by the reversible dissociation of the catalytic V(1) complex from the membrane bound proton translocating V(0) complex and, on the other hand, their high sensitivity to specific macrolides such as bafilomycin and concanamycin from streptomycetes or archazolid and apicularen from myxomycetes. Both features require distinct intramolecular as well as intermolecular interactions. Here we will summarize our own results together with newer developments in both of these research areas.
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