Interaction between subunit C (Vma5p) of the yeast vacuolar ATPase and the stalk of the C-depleted V(1) ATPase from Manduca sexta midgut.
Projection maps of a V(1)-Vma5p hybrid complex, composed of subunit C (Vma5p) of Saccharomyces cerevisiae V-ATPase and the C-depleted V(1) from Manduca sexta, were determined from single particle electron microscopy. V(1)-Vma5p consists of a headpiece and an elongated wedgelike stalk with a 2.1x3.0 nm protuberance and a 9.5x7.5 globular domain, interpreted to include Vma5p. The interaction face of Vma5p in V(1) was explored by chemical modification experiments.
Chaban
Yuriy L
YL
Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands.
Juliano
Sandra
S
Boekema
Egbert J
EJ
Grüber
Gerhard
G
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D018402:Manduca / Q000201:enzymology*; D008854:Microscopy, Electron; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000302:isolation & purification; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000302:isolation & purification
D029701:Saccharomyces cerevisiae Proteins; C447616:VMA5 protein, S cerevisiae; D025262:Vacuolar Proton-Translocating ATPases