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Plant Cell. 2018 Aug;30(8):1770-1788. doi: 10.1105/tpc.18.00075. Epub 2018 Jul 16.

Nucleus-Encoded Protein BFA1 Promotes Efficient Assembly of the Chloroplast ATP Synthase Coupling Factor 1.

Author information

1
College of Life and Environmental Sciences, Shanghai Normal University, Shanghai 200234, China.
2
Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
3
Departments of Molecular Biology and Plant Biology, University of Geneva, 1211 Geneva, Switzerland.
4
School of Life Sciences, Anhui University, Hefei, Anhui 230601, China.
5
College of Life and Environmental Sciences, Shanghai Normal University, Shanghai 200234, China penglianwei@shnu.edu.cn.

Abstract

F-type ATP synthases produce nearly all of the ATP found in cells. The catalytic module F1 commonly comprises an α3β3 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 CF1β, 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 CF1β 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 CF1β/γ. We propose that BFA1 acts mainly as a scaffold protein promoting the association of a CF1α/β heterodimer with CF1γ. The subsequent assembly of other CF1α/β heterodimers may shift the position of the CF1γ 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.

PMID:
30012777
PMCID:
PMC6139693
[Available on 2019-08-01]
DOI:
10.1105/tpc.18.00075

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