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Subunit Asa3 ensures the attachment of the peripheral stalk to the membrane sector of the dimeric ATP synthase of Polytomella sp.

Colina-Tenorio, Lilia, Miranda-Astudillo, Héctor, Dautant, Alain, Vázquez-Acevedo, Miriam, Giraud, Marie-France, González-Halphen, Diego
Biochemical and biophysical research communications 2019 v.509 no.2 pp. 341-347
H+/K+-exchanging ATPase, H-transporting ATP synthase, Western blotting, algae, dimerization, mitochondria, topology
The mitochondrial ATP synthase of Polytomella exhibits a peripheral stalk and a dimerization domain built by the Asa subunits, unique to chlorophycean algae. The topology of these subunits has been extensively studied. Here we explored the interactions of subunit Asa3 using Far Western blotting and subcomplex reconstitution, and found it associates with Asa1 and Asa8. We also identified the novel interactions Asa1-Asa2 and Asa1-Asa7. In silico analyses of Asa3 revealed that it adopts a HEAT repeat-like structure that points to its location within the enzyme based on the available 3D-map of the algal ATP synthase. We suggest that subunit Asa3 is instrumental in securing the attachment of the peripheral stalk to the membrane sector, thus stabilizing the dimeric mitochondrial ATP synthase.