HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 279, Issue 11, 9685-9688, March 12, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/11/9685    most recent C400014200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pavlova, P. Articles by Bald, D. Search for Related Content PubMed PubMed Citation Articles by Pavlova, P. Articles by Bald, D. Social Bookmarking                      What's this?

ACCELERATED PUBLICATIONS

Complete Inhibition and Partial Re-activation of Single F₁-ATPase Molecules by Tentoxin

NEW PROPERTIES OF THE RE-ACTIVATED ENZYME^*

Penka Pavlova, Katsuya Shimabukuro, Toru Hisabori, Georg Groth¶, Holger Lill, and Dirk Bald||

From the Department of Structural Biology, Faculty of Earth and Life Science, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands, the Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8503, Japan, and ^¶Plant Biochemistry, University of Duesseldorf, Universitaetsstrasse 1, D-40225 Duesseldorf, Germany

During hydrolysis of ATP, the subunit of the rotary motor protein F₁-ATPase rotates within a ring of ₃₃ subunits. Tentoxin is a phyto-pathogenic cyclic tetrapeptide, which influences F₁-ATPase activity of sensitive species. At low concentrations, tentoxin inhibits ATP hydrolysis of ensembles of F₁ molecules in solution. At higher concentrations, however, ATP hydrolysis recovers. Here we have examined how tentoxin acts on individual molecules of engineered F₁-ATPase from the thermophilic Bacillus PS3 (Groth, G., Hisabori, T., Lill, H., and Bald, D. (2002) J. Biol. Chem. 277, 20117–20119). We found that inhibition by tentoxin caused a virtually complete stop of rotation, which was partially relieved at higher tentoxin concentrations. Re-activation, however, was not simply a reversal of inhibition; while the torque appears unaffected as compared with the situation without tentoxin, F₁ under re-activating conditions was less susceptible to inhibitory ADP binding but displayed a large number of short pauses, indicating infringed energy conversion.

Received for publication, January 12, 2004

^* This work was supported by the Faculty of Earth and Life Science at the Vrije Universiteit Amsterdam. The costs of publication of this article were defrayed in part by the payment of page charges. This 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: Dept. of Structural Biology, Faculty of Earth and Life Science, Vrije Universiteit Amsterdam, De Boelelaan 1085, 1181 HV Amsterdam, The Netherlands. Tel.: 31-20-44-46991; Fax: 31-20-44-47136; E-mail: dirkbald{at}bio.vu.nl.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				H. Lill, T. Hisabori, G. Groth, and D. Bald A thermostable enzyme as an experimental platform to study properties of less stable homologues Protein Eng. Des. Sel., July 1, 2004; 17(7): 553 - 555. [Abstract] [Full Text] [PDF]