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Proton-Translocating ATPase (F1F0) of Escherichia coli

  • Masamitsu Futai
  • Hiroshi Kanazawa

Abstract

Studies on proton-translocating ATPase (F1F0) from Escherichia coli started much later than those on F1F0 from eukaryotic organelles such as mitochondria and chloroplasts. The F1-ATPase of E. coli was purified after solubilization from cytoplasmic membranes and was shown to have essentially the same function and five-subunit structure (α, β, γ, δ, ∈) as other F1’s. The entire F1F0 complex and F0 portion were also purified (for review see Futai and Kanazawa, 1980). In this review we discuss studies on F1F0 from E. coli, particularly the isolation of its subunits, the reconstitution of the complex, the identification of defective subunits in mutants, and the physical location of the genes in the bacterial chromosome. These recent findings show that techniques of molecular biology have led to detailed understanding of the complex.

Keywords

ATPase Activity Proton Channel Major Subunit Transduce Phage Study Amino Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Masamitsu Futai
    • 1
  • Hiroshi Kanazawa
    • 1
  1. 1.Department of Microbiology, Faculty of Pharmaceutical SciencesOkayama UniversityOkayama 700Japan

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