TY  - JOUR
A1  - Wittig, Ilka
A1  - Velours, Jean
A1  - Stuart, Rosemary
A1  - Schägger, Hermann
T1  - Characterization of domain interfaces in monomeric and dimeric ATP synthase
T2  - Molecular & Cellular Proteomics
N2  - We disassembled monomeric and dimeric yeast ATP synthase under mild conditions to identify labile proteins and transiently stable subcomplexes that had not been observed before. Specific removal of subunits α, β, oligomycin sensitivity conferring protein (OSCP), and h disrupted the ATP synthase at the γ-α3β3 rotor-stator interface. Loss of two F1-parts from dimeric ATP synthase led to the isolation of a dimeric subcomplex containing membrane and peripheral stalk proteins thus identifying the membrane/peripheral stalk sectors immediately as the dimerizing parts of ATP synthase. Almost all subunit a was found associated with a ring of 10 c-subunits in two-dimensional blue native/SDS gels. We therefore postulate that c10a1-complex is a stable structure in resting ATP synthase until the entry of protons induces a breaking of interactions and stepwise rotation of the c-ring relative to the a-subunit in the catalytic mechanism. Dimeric subunit a was identified in SDS gels in association with two c10-rings suggesting that a c10a2c10-complex may constitute an important part of the monomer-monomer interface in dimeric ATP synthase that seems to be further tightened by subunits b, i, e, g, and h. In contrast to the monomer-monomer interface, the interface between dimers in higher oligomeric structures remains largely unknown. However, we could show that the natural inhibitor protein Inh1 is not required for oligomerization.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76367
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-763678
SN  - 1535-9476
VL  - 7.2008
IS  - 5
SP  - 995
EP  - 1004
PB  - The American Society for Biochemistry and Molecular Biology
CY  - Bethesda, Md.
ER  -