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Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit

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Zhang,  Chunli
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Marcia,  Marco
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

Langer,  Julian D.
Max Planck Society;

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Peng,  Guohong
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Zhang, C., Marcia, M., Langer, J. D., Peng, G., & Michel, H. (2013). Role of the N-terminal signal peptide in the membrane insertion of Aquifex aeolicus F1F0 ATP synthase c-subunit. The FEBS Journal, 280(14), 3425-3435.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-D4BE-8
Abstract
Rotary ATPases are membrane protein complexes that couple ATP hydrolysis to ion translocation across the membrane. Overall, they are evolutionarily well conserved, but the N-terminal segments of their rotary subunits (c-subunits) possess different lengths and levels of hydrophobicity across species. By analyzing the N-terminal variability, we distinguish four phylogenetic groups of c-subunits (groups 1–4). We characterize a member of group 2, the c-subunit from Aquifex aeolicus F1F0 ATP synthase, both in native cells and in a heterologous expression system. We demonstrate that its N-terminal segment forms a signal peptide with signal recognition particle (SRP) recognition features and is obligatorily required for membrane insertion. Based on our study and on previous characterizations of c-subunits from other organisms, we propose that c-subunits follow different membrane insertion pathways.