5yvf

Publication Abstract from PubMed

F-type ATP synthases produce nearly all of the ATP found in cells. The catalytic module, F1, commonly comprises an alpha3beta3 hexamer surrounding a gamma/epsilon stalk. However, it is unclear how these subunits assemble to form a catalytic motor. In this work, we identified and characterized a chloroplast protein that interacts with the CF1beta, gamma, and epsilon subunits of the chloroplast ATP synthase and is required for assembly of its F1 module. We have named this protein BFA1 (BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 1) and determined its crystal structure at 2.8A resolution. BFA1 is comprised primarily of two interacting beta-barrels that are oriented nearly perpendicularly to each other. The contact region between BFA1 and the CF1beta and gamma subunits was further mapped by yeast two-hybrid assays. An in silico molecular docking analysis was performed and revealed close fitting contact sites without steric conflicts between BFA1 and CF1beta/gamma. We propose that BFA1 acts mainly as a scaffold protein promoting the association of a CF1alpha/beta heterodimer with CF1gamma. The subsequent assembly of other CF1alpha/beta heterodimers may shift the position of the CF1gamma subunit to complete assembly of the CF1 module. This CF1 assembly process is likely to be valid for other F-type ATP synthases, as their structures are highly conserved.

Nucleus-Encoded Protein BFA1 Promotes Efficient Assembly of the Chloroplast ATP Synthase Coupling Factor 1.,Zhang L, Pu H, Duan Z, Li Y, Liu B, Zhang Q, Li W, Rochaix JD, Liu L, Peng L Plant Cell. 2018 Jul 16. pii: tpc.18.00075. doi: 10.1105/tpc.18.00075. PMID:30012777^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.