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

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. doi:10.1111/febs.12336.

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 Creators:
Zhang, Chunli1, Author              
Marcia, Marco2, Author
Langer, Julian David1, Author              
Peng, Guohong1, 3, Author              
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT, USA, ou_persistent22              
3Institute of Oceanology, Chinese Academy of Sciences, Qingdao, China, ou_persistent22              

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Free keywords: energy conservation; membrane insertion; membrane topology; rotary ATPases; signal peptide
 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.

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Language(s): eng - English
 Dates: 2013-05-032013-03-172013-05-072013-05-112013-07
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1111/febs.12336
 Degree: -

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Title: The FEBS Journal
  Other : The Federation if European Biochemical Societies Journal
Source Genre: Journal
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Publ. Info: Wiley-Blackwell
Pages: - Volume / Issue: 280 (14) Sequence Number: - Start / End Page: 3425 - 3435 Identifier: ISSN: 1742-464X
CoNE: https://pure.mpg.de/cone/journals/resource/954925398485