UncI protein can mediate ring-assembly of c-subunits of FoF1-ATP synthase in vitro

Biochemical and Biophysical Research Communications
Yoko OzakiMasasuke Yoshida

Abstract

In F(o)F(1)-ATP synthase, multimeric c-subunits are assembled to a ring (c-ring) in the membranes that rotates as protons flow across F(o). We recently reported that assembly of c-ring of Propionigenium modestum in the membranes of Escherichia coli cells required P. modestum UncI, a product of the conserved uncI gene in the F(o)F(1) operon. However, cooperation with endogenous factors in E. coli remained unclear. Here, P. modestum c-subunit was synthesized in vitro in the presence of liposomes. When c-subunit alone was synthesized, it did not form c-ring. However, when c-subunit and P. modestum UncI were synthesized together, c-ring was formed. Fusion of the two kinds of liposomes, one containing only unassembled c-subunit and the other only UncI, resulted in gradual formation of c-ring. Thus, UncI alone can mediate in vitro post-translational c-ring assembly.

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Citations

Oct 12, 2012·Journal of Bioenergetics and Biomembranes·Karsten BrandtVolker Müller
Jul 10, 2013·Journal of Bacteriology·Britta BrockmannGabriele Deckers-Hebestreit
Jun 6, 2009·Annual Review of Biochemistry·Christoph von BallmoosPeter Dimroth
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Mar 7, 2020·Biological Chemistry·Leticia Veloso Ribeiro FrancoAlexander Tzagoloff
Dec 19, 2019·Frontiers in Molecular Biosciences·Olga NovitskaiaIvan Gushchin
Nov 2, 2019·Mitochondrion·Mario H Barros, Gavin P McStay

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