Functional production of the Na+ F1FO ATP synthase from Acetobacterium woodii in Escherichia coli requi

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• 作者：Karsten Brandt (1)
  Daniel B. Müller (1)
  Jan Hoffmann (2)
  Christine Hübert (3)
  Bernd Brutschy (2)
  Gabriele Deckers-Hebestreit (3)
  Volker Müller (1)
  
• 关键词：AtpI ; ATP synthase ; Sodium transport ; Membrane enzymes ; Bioenergetics ; Hybrid rotor
• 刊名：Journal of Bioenergetics and Biomembranes
• 出版年：2013
• 出版时间：2 - February 2013
• 年：2013
• 卷：45
• 期：1
• 页码：15-23
• 全文大小：390KB
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• 作者单位：Karsten Brandt (1)
  Daniel B. Müller (1)
  Jan Hoffmann (2)
  Christine Hübert (3)
  Bernd Brutschy (2)
  Gabriele Deckers-Hebestreit (3)
  Volker Müller (1)
  
  1. Molecular Microbiology & Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt/Main, Max-von-Laue-Str. 9, 60438, Frankfurt, Germany
  2. Institute for Physical and Theoretical Chemistry, Johann Wolfgang Goethe University Frankfurt/Main, Max-von-Laue Str. 7, 60438, Frankfurt, Germany
  3. Microbiology, Department of Biology/Chemistry, University of Osnabrück, Barbarastra?e 11, 49069, Osnabrück, Germany
  
• ISSN：1573-6881

文摘

The Na+ F1FO ATP synthase of the anaerobic, acetogenic bacterium Acetobacterium woodii has a unique FOVO hybrid rotor that contains nine copies of a FO-like c subunit and one copy of a VO-like c 1 subunit with one ion binding site in four transmembrane helices whose cellular function is obscure. Since a genetic system to address the role of different c subunits is not available for this bacterium, we aimed at a heterologous expression system. Therefore, we cloned and expressed its Na+ F1FO ATP synthase operon in Escherichia coli. A Δatp mutant of E. coli produced a functional, membrane-bound Na+ F1FO ATP synthase that was purified in a single step after inserting a His6-tag to its β subunit. The purified enzyme was competent in Na+ transport and contained the FOVO hybrid rotor in the same stoichiometry as in A. woodii. Deletion of the atpI gene from the A. woodii operon resulted in a loss of the c ring and a mis-assembled Na+ F1FO ATP synthase. AtpI from E. coli could not substitute AtpI from A. woodii. These data demonstrate for the first time a functional production of a FOVO hybrid rotor in E. coli and revealed that the native AtpI is required for assembly of the hybrid rotor.