Nucleus-Encoded Protein BFA1 Promotes Efficient Assembly of the Chloroplast ATP Synthase Coupling Factor 1. Issue 8 (16th July 2018)

• Record Type: Journal Article
• Authors: Zhang, Lin; Pu, Hua; Duan, Zhikun; Li, Yonghong; Liu, Bei; Zhang, Qiqi; Li, Wenjing; Rochaix, Jean-David; Liu, Lin; Peng, Lianwei
• Is Part Of: The Plant Cell. Volume 30:Issue 8(2018)
• Page Start: 1770
• Page End: 1788
• Publication Date: 2018-07-16
• DOI: 10.1105/tpc.18.00075
• Languages: English
• ISSNs: 1040-4651

Abstract

Abstract : Chloroplast protein BFA1 is comprised primarily of two β-barrels and acts as a chaperone orchestrating the early steps of the CF1 assembly pathway via specific interaction with the CF1 β, γ, and ε subunits. Abstract: F-type ATP synthases produce nearly all of the ATP found in cells. The catalytic module F1 commonly comprises an α3 β3 hexamer surrounding a γ/ε 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 CF1 β, γ, and ε subunits of the chloroplast ATP synthase and is required for assembly of its F1 module. We named this protein BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE1 (BFA1) and determined its crystal structure at 2.8-Å resolution. BFA1 is comprised primarily of two interacting β-barrels that are oriented nearly perpendicularly to each other. The contact region between BFA1 and the CF1 β and γ 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 CF1 β/γ. We propose that BFA1 acts mainly as a scaffold protein promoting the association of a CF1 α/β heterodimer with CF1 γ. The subsequent assembly of other CF1 α/β heterodimers may shift the position of the CF1 γ 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.