Bioenergetics pp 205-216 | Cite as

Situation of Archaebacterial ATPase among Ion-Translocating ATPases

  • Yasuo Mukohata
  • Kunio Ihara


Among the ATPases so far isolated from archaebacteria, only the halobacterial ATPase has been proven to be the (catalytic) part of ATP synthase. This ATPase/synthase is H+-translocating and has unique chracteristics as enzyme/protein.

An antibody raised against this halobacterial ATPase cross-reacted to the ATPases from other archaebacteria, thermoacidophile and methanogen. From various additional points of view, all the archaebacterial ATPases can be regarded as a family, and categolized into “A-type” ATPase (Archae-ATP-synthase)2).

Immunoblotting also showed that the A-type ATPase is close to the V-type one, so-called anion-sensitive H+-ATPase e.g., of vacuolar membranes (specifically sensitive to nitrate). This finding would support the concept of endosymbiotic evolution with a primitive archaebacterium as the host. In contrast, the A-type ATPase, esp. of halobacteria, was found to be very much less related to the F-type ATPase (i.e., F0F1 ATP synthase) or to the P-type (e.g., Na,K-ATPase and Ca2+-ATPase) than the V-type one. This finding together with unique characteristics of the A-type ATPase, such as azide insensitivity, made the halobacterial ATP synthase the first exception from the common understanding that the F-type ATPase is present ubiquitously in all aerobic organisms to synthesize ATP.

The amino acid sequences deduced from the DNA sequences of the cloned genes for the ATPases of halobacteria and other archaebacteria, fully confirmed the immunoblotting data described above.

On the basis of these observations an attempt is made to discuss the evolution of H+-ATPase.


Rabbit Skeletal Muscle Methanosarcina Barkeri Sulfolobus Acidocaldarius Head Piece Halobacterium Salinarium 
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 1990

Authors and Affiliations

  • Yasuo Mukohata
    • 1
  • Kunio Ihara
    • 1
  1. 1.Department of Biology, Faculty of ScienceNagoya UniversityNagoyaJapan

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