JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M100289200 on February 13, 2001

J. Biol. Chem., Vol. 276, Issue 18, 15269-15274, May 4, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/18/15269    most recent
M100289200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tanabe, M.
Right arrow Articles by Futai, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tanabe, M.
Right arrow Articles by Futai, M.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Rotation of a Complex of the gamma  Subunit and c Ring of Escherichia coli ATP Synthase
THE ROTOR AND STATOR ARE INTERCHANGEABLE*

Mikio TanabeDagger , Kazuaki NishioDagger , Yuko IkoDagger , Yoshihiro SambongiDagger , Atsuko Iwamoto-Kihara§, Yoh WadaDagger , and Masamitsu FutaiDagger

From the Dagger  Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan and the § Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Komaba, Tokyo 153-8902, Japan

ATP synthase (F0F1) transforms an electrochemical proton gradient into chemical energy (ATP) through the rotation of a subunit assembly. It has been suggested that a complex of the gamma  subunit and c ring (c10-14) of F0F1 could rotate together during ATP hydrolysis and synthesis (Sambongi, Y., Iko, Y., Tanabe, M., Omote, H., Iwamoto-Kihara, A., Ueda, I., Yanagida, T., Wada, Y., and Futai, M. (1999) Science 286, 1722-1724). We observed that the rotation of the c ring with the cI28T mutation (c subunit cIle-28 replaced by Thr) was less sensitive to venturicidin than that of the wild type, consistent with the antibiotic effect on the cI28T mutant and wild-type ATPase activities (Fillingame, R. H., Oldenburg, M., and Fraga, D. (1991) J. Biol. Chem. 266, 20934-20939). Furthermore, we engineered F0F1 to see the alpha 3beta 3 hexamer rotation; a biotin tag was introduced into the alpha  or beta  subunit, and a His tag was introduced into the c subunit. The engineered enzymes could be purified by metal affinity chromatography and density gradient centrifugation. They were immobilized on a glass surface through the c subunit, and an actin filament was connected to the alpha  or beta  subunit. The filament rotated upon the addition of ATP and generated essentially the same frictional torque as one connected to the c ring. These results indicate that the gamma epsilon c10-14 complex is a mechanical unit of the enzyme and that it can be used as a rotor or a stator experimentally, depending on the subunit immobilized.

* This work was supported in part by the Japanese Ministry of Education, Science, and Culture.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Div. of Biological Sciences, ISIR, Osaka University, Ibaraki, Osaka 567-0047, Japan. Tel.: 81-6-6879-8480; Fax: 81-6-6875-5724; E-mail: m-futai@sanken.osaka-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
J. A. B. Scanlon, M. K. Al-Shawi, and R. K. Nakamoto
A Rotor-Stator Cross-link in the F1-ATPase Blocks the Rate-limiting Step of Rotational Catalysis
J. Biol. Chem., September 19, 2008; 283(38): 26228 - 26240.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Nakanishi-Matsui, S. Kashiwagi, T. Ubukata, A. Iwamoto-Kihara, Y. Wada, and M. Futai
Rotational Catalysis of Escherichia coli ATP Synthase F1 Sector: STOCHASTIC FLUCTUATION AND A KEY DOMAIN OF THE beta SUBUNIT
J. Biol. Chem., July 13, 2007; 282(28): 20698 - 20704.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Nakanishi-Matsui, S. Kashiwagi, H. Hosokawa, D. J. Cipriano, S. D. Dunn, Y. Wada, and M. Futai
Stochastic High-speed Rotation of Escherichia coli ATP Synthase F1 Sector: THE {epsilon} SUBUNIT-SENSITIVE ROTATION
J. Biol. Chem., February 17, 2006; 281(7): 4126 - 4131.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Hosokawa, M. Nakanishi-Matsui, S. Kashiwagi, I. Fujii-Taira, K. Hayashi, A. Iwamoto-Kihara, Y. Wada, and M. Futai
ATP-dependent Rotation of Mutant ATP Synthases Defective in Proton Transport
J. Biol. Chem., June 24, 2005; 280(25): 23797 - 23801.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Puri, J. Lai-Zhang, S. Meier, and D. M. Mueller
Expression of Bovine F1-ATPase with Functional Complementation in Yeast Saccharomyces cerevisiae
J. Biol. Chem., June 10, 2005; 280(23): 22418 - 22424.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Ueno, T. Suzuki, K. Kinosita Jr., and M. Yoshida
ATP-driven stepwise rotation of FoF1-ATP synthase
PNAS, February 1, 2005; 102(5): 1333 - 1338.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
H. Richard and J. W. Foster
Escherichia coli Glutamate- and Arginine-Dependent Acid Resistance Systems Increase Internal pH and Reverse Transmembrane Potential
J. Bacteriol., September 15, 2004; 186(18): 6032 - 6041.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
A. Aksimentiev, I. A. Balabin, R. H. Fillingame, and K. Schulten
Insights into the Molecular Mechanism of Rotation in the Fo Sector of ATP Synthase
Biophys. J., March 1, 2004; 86(3): 1332 - 1344.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G.-H. Sun-Wada, Y. Murata, M. Namba, A. Yamamoto, Y. Wada, and M. Futai
Mouse Proton Pump ATPase C Subunit Isoforms (C2-a and C2-b) Specifically Expressed in Kidney and Lung
J. Biol. Chem., November 7, 2003; 278(45): 44843 - 44851.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Hirata, A. Iwamoto-Kihara, G.-H. Sun-Wada, T. Okajima, Y. Wada, and M. Futai
Subunit Rotation of Vacuolar-type Proton Pumping ATPase: RELATIVE ROTATION OF THE G AND c SUBUNITS
J. Biol. Chem., June 20, 2003; 278(26): 23714 - 23719.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
K. Nishio, A. Iwamoto-Kihara, A. Yamamoto, Y. Wada, and M. Futai
Subunit rotation of ATP synthase embedded in membranes: a or beta subunit rotation relative to the c subunit ring
PNAS, October 15, 2002; 99(21): 13448 - 13452.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Murata, G.-H. Sun-Wada, T. Yoshimizu, A. Yamamoto, Y. Wada, and M. Futai
Differential Localization of the Vacuolar H+ Pump with G Subunit Isoforms (G1 and G2) in Mouse Neurons
J. Biol. Chem., September 20, 2002; 277(39): 36296 - 36303.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. J. Cipriano, Y. Bi, and S. D. Dunn
Genetic Fusions of Globular Proteins to the epsilon Subunit of the Escherichia coli ATP Synthase. IMPLICATIONS FOR IN VIVO ROTATIONAL CATALYSIS AND epsilon SUBUNIT FUNCTION
J. Biol. Chem., May 3, 2002; 277(19): 16782 - 16790.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Iko, Y. Sambongi, M. Tanabe, A. Iwamoto-Kihara, K. Saito, I. Ueda, Y. Wada, and M. Futai
ATP Synthase F1 Sector Rotation. DEFECTIVE TORQUE GENERATION IN THE beta SUBUNIT SER-174 TO PHE MUTANT AND ITS SUPPRESSION BY SECOND MUTATIONS
J. Biol. Chem., December 7, 2001; 276(50): 47508 - 47511.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.