Association of the eukaryotic V1VO ATPase subunits a with d and d with A.
Owing to the complex nature of V(1)V(O) ATPases, identification of neighboring subunits is essential for mechanistic understanding of this enzyme. Here, we describe the links between the V(1) headpiece and the V(O)-domain of the yeast V(1)V(O) ATPase via subunit A and d as well as the V(O) subunits a and d using surface plasmon resonance and fluorescence correlation spectroscopy. Binding constants of about 60 and 200 nM have been determined for the a-d and d-A assembly, respectively. The data are discussed in light of subunit a and d forming a peripheral stalk, connecting the catalytic A(3)B(3) hexamer with V(O).
Thaker
Youg R
YR
School of Biological Sciences, Nanyang Technological University, Singapore 637551, Republic of Singapore.
Hunke
Cornelia
C
Yau
Yin H
YH
Shochat
Susana Geifman
SG
Li
Ying
Y
Grüber
Gerhard
G
D020836:Protein Structure, Quaternary / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry*
D029701:Saccharomyces cerevisiae Proteins; D025262:Vacuolar Proton-Translocating ATPases