Situation of Archaebacterial ATPase among Ion-Translocating ATPases
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.
KeywordsRabbit Skeletal Muscle Methanosarcina Barkeri Sulfolobus Acidocaldarius Head Piece Halobacterium Salinarium
Unable to display preview. Download preview PDF.
- 3.Larsen, H.(1984) in “Bergey's Mannual of Systematic Bacteriology” 9th edition (Krieg, N.R. ed.) pp 261–267, Williams & Wilkins, BaltimoreGoogle Scholar
- 11.Ihara, K. and Mukohata, Y. submittedGoogle Scholar
- 12.Mukohata, Y., Matsuno-Yagi and Kaji, Y. (1980) in “Saline Environment” (Morishita, M. & Masui, M. eds.) pp31–37, Business Center Acad. Soc. Japan, TokyoGoogle Scholar
- 19.Maniatis, R.T., Fritsh, E.F. and Sambrook, J. (1982) Molecular Cloning-a laboratory mannual, Cold Spring Harbor Lab., New YorkGoogle Scholar
- 24.Mukohata, Y., Isoyama, M., Fuke, A., Sugiyama, Y. Ihara, K., Yoshida, M. and Nanba, T. (1987) in “Perspectives of Biological Energy Transduction” (Mukohata, Y., Morales, M.F. & Fleischer, S. eds.) pp 331–338, Academic Press, TokyoGoogle Scholar
- 40.Konishi, J., Oshima, T., Wakagi, T., Uchida, E., Ohsumi, Y., Anraku, Y., Matsumoto, T., Wakabayashi, T., Mukohata, Y., Ihara, K., Inatomi, K., Kato, K., Ohta, T., Allison, W.S. and Yoshida, M. (1989) J. Biochem. in pressGoogle Scholar
- 46.Okutani, S.Y., Ihara, K. and Mukohata, Y. submittedGoogle Scholar
- 49.Percy, J.M. and Apps, D.K. (1981) Biochem. J. 239, 77–81Google Scholar
- 51.Mandala, S. and Taiz, L. (1987) J. Biol. Chem. 262, 15780–15789Google Scholar