JBC Origene Your Gene Company

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


     


Originally published In Press as doi:10.1074/jbc.M111678200 on June 3, 2002

J. Biol. Chem., Vol. 277, Issue 35, 31287-31290, August 30, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/35/31287    most recent
M111678200v1
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 Gumbiowski, K.
Right arrow Articles by Engelbrecht, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gumbiowski, K.
Right arrow Articles by Engelbrecht, S.
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 the c Subunit Oligomer in EF0EF1 Mutant cD61N*

Karin Gumbiowski, Oliver Pänke, Wolfgang Junge, and Siegfried EngelbrechtDagger

From the Universität Osnabrück, FB Biologie, Abt. Biophysik, Barbarastrasse 11, 49076 Osnabrück, Germany

ATP synthases (F0F1-ATPases) mechanically couple ion flow through the membrane-intrinsic portion, F0, to ATP synthesis within the peripheral portion, F1. The coupling most probably occurs through the rotation of a central rotor (subunits c10epsilon gamma ) relative to the stator (subunits ab2delta (alpha beta )3). The translocation of protons is conceived to involve the rotation of the ring of c subunits (the c oligomer) containing the essential acidic residue cD61 against subunits ab2. In line with this notion, the mutants cD61N and cD61G have been previously reported to lack proton translocation. However, it has been surprising that the membrane-bound mutated holoenzyme hydrolyzed ATP but without translocating protons. Using detergent-solubilized and immobilized EF0F1 and by application of the microvideographic assay for rotation, we found that the c oligomer, which carried a fluorescent actin filament, rotates in the presence of ATP in the mutant cD61N just as in the wild type enzyme. This observation excluded slippage among subunit gamma , the central rotary shaft, and the c oligomer and suggested free rotation without proton pumping between the oligomer and subunit a in the membrane-bound enzyme.


* This work was supported by grants from the Deutsche Forshungsgemeinschaft (SFB 431/D1) (to W. J. and S. E.) and by the Human Sciences Frontier Project (to W. J.).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.

Dagger To whom correspondence should be addressed. Fax: 49-541-969-2870; E-mail: engel@uos.de.


Copyright © 2002 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
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 HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.