Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Mimura, H.
Right arrow Articles by Tagawa, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mimura, H.
Right arrow Articles by Tagawa, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1993, Vol. 113, No. 3 350-354
© 1993 Japanese Biochemical Society

research-article

Binding of an Intrinsic ATPase Inhibitor to the Interface between {alpha}and ß-Subunits of FiFoATPase upon De-Energization of Mitochondria1

Haruo Mimura*,2,3, Tadao Hashimoto**, Yukuo Yoshida*, Naoki Ichikawa*,2 and Kunio Tagawa*,2

*Department of Physiological Chemistry, Medical School, Osaka University Suita, Yamadaoka, Osaka 565;
**Muroran Institute of Technology Muroran, Hokkaido 050

2Kobe Mercantile Marine University Fukae-Minami-cho, Higashinada-ku, Kobe, Hyogo 658

3To Whom correspondence should be addressed

Yeast mitochondrial FiFoATPase has three regulatory subunit proteins: ATPase inhibitor, 9K protein, and 15K protein. Mutant yeasts lacking one or more of these protein factors were constructed by gene disruption [Ichikawa, N. et aL (1990) J. BioL Chem. 265, 6274-6278; Yoshida, Y. et al. (1990) Eur. J. Biochem. 193, 49-53]. Dissipation of the electrochemical potential of protons of the mitochondrial inner membrane by an uncoupler or by a combination of valinomycin and potassium ions induced ATP-hydrolyzing activity of FiFoATPase in mitochondria of all the mutants, as in those of wild-type cells. However, the ATPase activity was inactivated within a minute in normal mitochondria, but was not suppressed in inhibitor-deficient mitochondria, and in mitochondria lacking either 9K or 15K protein, the inactivation of ATPase was slow and incomplete. Covalent binding of inhibitor protein to the enzyme was achieved with a zero length cross-linker, EEDQ, in uncoupled normal mitochondria, in which the inhibitor linked directly to both the a- and ;9-subunits. This result strongly suggests that the binding site of the inhibitor protein is located at the interface between the two subunits.

1This research was partly supported by a Grant-in-Aid for Scientific Research (No. 04680151) and a Grant-in-Aid for Scientific Research on a Priority Area (No. 04266104) to K.T. from the Ministry of Education, Science and Culture of Japan

2Department of Food and Nutrition, Faculty of Science of Living, Osaka City University 3-138 Sugimoto-cho, Sumiyoshi-kn, Osaka 558


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
V. Corvest, C. Sigalat, R. Venard, P. Falson, D. M. Mueller, and F. Haraux
The Binding Mechanism of the Yeast F1-ATPase Inhibitory Peptide: ROLE OF CATALYTIC INTERMEDIATES AND ENZYME TURNOVER
J. Biol. Chem., March 18, 2005; 280(11): 9927 - 9936.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Krippner, A. Matsuno-Yagi, R. A. Gottlieb, and B. M. Babior
Loss of Function of Cytochrome c in Jurkat Cells Undergoing Fas-mediated Apoptosis
J. Biol. Chem., August 30, 1996; 271(35): 21629 - 21636.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.