Abstract:
: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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Colina-Tenorio L,Miranda-Astudillo H,Dautant A,Vázquez-Acevedo M,Giraud MF,González-Halphen Ddoi
10.1016/j.bbrc.2018.12.142subject
Has Abstractpub_date
2019-02-05 00:00:00pages
341-347issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(18)32807-9journal_volume
509pub_type
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