UncI protein can mediate ring-assembly of c-subunits of FoF1-ATP synthase in vitro |
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Authors: | Ozaki Yoko Suzuki Toshiharu Kuruma Yutetsu Ueda Takuya Yoshida Masasuke |
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Institution: | a Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8503, Japan b ATP Synthesis Regulation Project, ICORP, Japan Science and Technology Corporation (JST), Aomi 2-41, Koto-ku, Tokyo 135-0064, Japan c Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba 277-8562, Japan |
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Abstract: | In FoF1-ATP synthase, multimeric c-subunits are assembled to a ring (c-ring) in the membranes that rotates as protons flow across Fo. 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 FoF1 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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Keywords: | ATP synthase Chaperone c-Subunit Motor enzyme Biogenesis of ATP synthase In vitro protein synthesis UncI YidC Membrane integration Membrane proteins |
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