Archaebacterial ATPases: Relationship to Other Ion-Translocating ATPase Families Examined in Terms of Immunological Cross-Reactivity

Immunological cross-reactivity among three types of H+-ATPases, that is, three archaebacterial ATPases, the F1-ATPase from thermophilic bacterium PS3 (TF1 and the vacuolar membrane ATPase from Saccharomyces cerevisiae, was examined by means of immunoblot analyses. The three archaebacterial ATPases w...

Full description

Saved in:
Bibliographic Details
Published inJournal of biochemistry (Tokyo) Vol. 108; no. 4; pp. 554 - 559
Main Authors Konishi, Jin, Denda, Kimitoshi, Oshima, Tairo, Wakagi, Takayoshi, Uchida, Etsuko, Ohsumi, Yoshinori, Anraku, Yasuhiro, Matsumoto, Takao, Wakabayashi, Takeyuki, Mukohata, Yasuo, Ihara, Kunio, Ken-ichi, Inatomi, Kato, Keitaro, Ohta, Toshiko, William, S. Allison, Yoshida, Masasuke
Format Journal Article
LanguageEnglish
Published Oxford Oxford University Press 01.10.1990
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Immunological cross-reactivity among three types of H+-ATPases, that is, three archaebacterial ATPases, the F1-ATPase from thermophilic bacterium PS3 (TF1 and the vacuolar membrane ATPase from Saccharomyces cerevisiae, was examined by means of immunoblot analyses. The three archaebacterial ATPases were very similar in immunological cross-reactivity, suggesting that they belong to the same family of ATPases. Cross-reaction was also observed between the ATPase from Sulfolobus acidocaldarius, one of the three archaebacteria, and TF1. S. cerevisiae vacuolar ATPase reacted with the antibodies prepared against each of the three archaebacterial ATPases, but did not react with the antibody against TF1. Electron microscopic examination revealed that the oligomeric structure of Sulfolobus ATPase was very similar to that of F1 -ATPase. These results, taken together, suggest that the archaebacterial ATPases share close structural similarities with the vacuolar ATPases, and, to a lesser degree, with the F0F1-ATPases.
Bibliography:istex:B9679BEE0270A28CBE888AA7D4BEF24FCD44E930
ArticleID:108.4.554
ark:/67375/HXZ-C0D8WGCX-K
1This work was partially supported by a Grant-in-Aid for Scientific Research on the Priority Area of “Bioenergetics” to M. Y. from the Ministry of Education, Science and Culture of Japan.
2To whom correspondence should be addressed
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a123241