JBC INTERFERin siRNA transfection reagent

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


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Anderson, V. E.
Right arrow Articles by Osheroff, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Anderson, V. E.
Right arrow Articles by Osheroff, N.
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?

J Biol Chem, Vol. 273, Issue 28, 17879-17885, July 10, 1998

Topoisomerase IV Catalysis and the Mechanism of Quinolone Action

Virginia E. AndersonDagger , Thomas D. Gootz, and Neil OsheroffDagger parallel

From the Departments of Dagger  Biochemistry and parallel  Medicine (Oncology), Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, and the  Department of Cancer, Immunology, and Infectious Diseases, Pfizer Central Research, Pfizer, Inc., Groton, Connecticut 06340

Topoisomerase IV is a bacterial type II topoisomerase that is essential for proper chromosome segregation and is a target for quinolone-based antimicrobial agents. Despite the importance of this enzyme to the survival of prokaryotic cells and to the treatment of bacterial infections, relatively little is known about the details of its catalytic mechanism or the basis by which quinolones alter its enzymatic functions. Therefore, a series of experiments that analyzed individual steps of the topoisomerase IV catalytic cycle were undertaken to address these critical mechanistic issues. The following conclusions were drawn. First, equilibrium levels of DNA cleavage mediated by the bacterial enzyme were considerably (>10-fold) higher than those observed with its eukaryotic counterparts. To a large extent, this reflected decreased rates of DNA religation. Second, the preference of topoisomerase IV for catalyzing DNA decatenation over relaxation reflects increased rates of strand passage and enzyme recycling rather than a heightened recognition of intermolecular DNA helices. Third, quinolones stimulate topoisomerase IV-mediated DNA cleavage both by increasing rates of DNA scission and by inhibiting religation of cleaved DNA. Finally, quinolones inhibit the overall catalytic activity of topoisomerase IV primarily by interfering with enzyme-ATP interactions.

Copyright © 1998 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. Bacteriol.Home page
P. Dupont, A. Aubry, E. Cambau, and L. Gutmann
Contribution of the ATP Binding Site of ParE to Susceptibility to Novobiocin and Quinolones in Streptococcus pneumoniae
J. Bacteriol., February 15, 2005; 187(4): 1536 - 1540.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
D. Ince and D. C. Hooper
Quinolone Resistance Due to Reduced Target Enzyme Expression
J. Bacteriol., December 1, 2003; 185(23): 6883 - 6892.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
F. Sifaoui, V. Lamour, E. Varon, D. Moras, and L. Gutmann
ATP-Bound Conformation of Topoisomerase IV: a Possible Target for Quinolones in Streptococcus pneumoniae
J. Bacteriol., October 15, 2003; 185(20): 6137 - 6146.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
O. A. Pierrat and A. Maxwell
The Action of the Bacterial Toxin Microcin B17: INSIGHT INTO THE CLEAVAGE-RELIGATION REACTION OF DNA GYRASE
J. Biol. Chem., September 12, 2003; 278(37): 35016 - 35023.
[Abstract] [Full Text] [PDF]

Home page
 Antimicrob. Agents Chemother.Home page
D. Strumberg, J. L. Nitiss, J. Dong, J. Walker, M. C. Nicklaus, K. W. Kohn, J. G. Heddle, A. Maxwell, S. Seeber, and Y. Pommier
Importance of the Fourth Alpha-Helix within the CAP Homology Domain of Type II Topoisomerase for DNA Cleavage Site Recognition and Quinolone Action
Antimicrob. Agents Chemother., September 1, 2002; 46(9): 2735 - 2746.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
R. W. Deibler, S. Rahmati, and E. L. Zechiedrich
Topoisomerase IV, alone, unknots DNA in E. coli
Genes & Dev., March 15, 2001; 15(6): 748 - 761.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
V. E. Anderson, R. P. Zaniewski, F. S. Kaczmarek, T. D. Gootz, and N. Osheroff
Quinolones Inhibit DNA Religation Mediated by Staphylococcus aureus Topoisomerase IV. CHANGES IN DRUG MECHANISM ACROSS EVOLUTIONARY BOUNDARIES
J. Biol. Chem., December 10, 1999; 274(50): 35927 - 35932.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. E. Shea and H. Hiasa
Interactions between DNA Helicases and Frozen Topoisomerase IV-Quinolone-DNA Ternary Complexes
J. Biol. Chem., August 6, 1999; 274(32): 22747 - 22754.
[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 © 1998 by the American Society for Biochemistry and Molecular Biology.