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

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.

authors

Colina-Tenorio L,Miranda-Astudillo H,Dautant A,Vázquez-Acevedo M,Giraud MF,González-Halphen D

doi

10.1016/j.bbrc.2018.12.142

subject

Has Abstract

pub_date

2019-02-05 00:00:00

pages

341-347

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(18)32807-9

journal_volume

509

pub_type

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