Unknown

Dataset Information

0

Interaction with monomeric subunit c drives insertion of ATP synthase subunit a into the membrane and primes a-c complex formation.


ABSTRACT: Subunit a is the main part of the membrane stator of the ATP synthase molecular turbine. Subunit c is the building block of the membrane rotor. We have generated two molecular fusions of a and c subunits with different orientations of the helical hairpin of subunit c. The a/c fusion protein with correct orientation of transmembrane helices was inserted into the membrane, and co-incorporated into the F(0) complex of ATP synthase with wild type subunit c. The fused c subunit was incorporated into the c-ring tethering the ATP synthase rotor to the stator. The a/c fusion with incorrect orientation of the c-helices required wild type subunit c for insertion into the membrane. In this case, the fused c subunit remained on the periphery of the c-ring and did not interfere with rotor movement. Wild type subunit a inserted into the membrane equally well with wild type subunit c and c-ring assembly mutants that remained monomeric in the membrane. These results show that interaction with monomeric subunit c triggers insertion of subunit a into the membrane, and initiates formation of the a-c complex, the ion-translocating module of the ATP synthase. Correct assembly of the ATP synthase incorporating topologically correct fusion of subunits a and c validates using this model protein for high resolution structural studies of the ATP synthase proton channel.

SUBMITTER: Pierson HE 

PROVIDER: S-EPMC3207401 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Interaction with monomeric subunit c drives insertion of ATP synthase subunit a into the membrane and primes a-c complex formation.

Pierson Hannah E HE   Uhlemann Eva-Maria E EE   Dmitriev Oleg Y OY  

The Journal of biological chemistry 20110907 44


Subunit a is the main part of the membrane stator of the ATP synthase molecular turbine. Subunit c is the building block of the membrane rotor. We have generated two molecular fusions of a and c subunits with different orientations of the helical hairpin of subunit c. The a/c fusion protein with correct orientation of transmembrane helices was inserted into the membrane, and co-incorporated into the F(0) complex of ATP synthase with wild type subunit c. The fused c subunit was incorporated into  ...[more]

Similar Datasets

| S-EPMC8698299 | biostudies-literature
| S-EPMC5701199 | biostudies-literature
| S-EPMC5059426 | biostudies-literature
| S-EPMC4059140 | biostudies-literature
| S-EPMC4893482 | biostudies-literature
| S-EPMC2172039 | biostudies-literature
| S-EPMC263739 | biostudies-literature
| S-EPMC2500151 | biostudies-literature
| S-EPMC10273367 | biostudies-literature
| S-EPMC3101027 | biostudies-literature