Skip Navigation

Nucleic Acids Research 2004 32(15):4596-4608; doi:10.1093/nar/gkh755
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (871K) Freely available
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 ISI Web of Science
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 Search for citing articles in:
ISI Web of Science (10)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Cannon, W. V.
Right arrow Articles by Buck, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cannon, W. V.
Right arrow Articles by Buck, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 27 August 2004

Nucleic Acids Research, Vol. 32 No. 15 © Oxford University Press 2004; all rights reserved

Nucleotide-dependent interactions between a fork junction–RNA polymerase complex and an AAA+ transcriptional activator protein

W. V. Cannon, J. Schumacher and M. Buck*

Department of Biological Sciences, Sir Alexander Fleming Building, Imperial College London, South Kensington Campus, London SW7 2AZ, UK

* To whom correspondence should be addressed. Tel: +44 207 594 5442; Fax: +44 207 594 5419; Email: m.buck{at}imperial.ac.uk

Received May 27, 2004; Revised July 14, 2004; Accepted July 21, 2004

Enhancer-dependent transcriptional activators that act upon the {sigma}54 bacterial RNA polymerase holoenzyme belong to the extensive AAA+ superfamily of mechanochemical ATPases. Formation and collapse of the transition state for ATP hydrolysis engenders direct interactions between AAA+ activators and the {sigma}54 factor, required for RNA polymerase isomerization. A DNA fork junction structure present within closed complexes serves as a nucleation point for the DNA melting seen in open promoter complexes and restricts spontaneous activator-independent RNA polymerase isomerization. We now provide physical evidence showing that the ADP·AlFx bound form of the AAA+ domain of the transcriptional activator protein PspF changes interactions between {sigma}54-RNA polymerase and a DNA fork junction structure present in the closed promoter complex. The results suggest that one functional state of the nucleotide-bound activator serves to alter DNA binding by {sigma}54 and {sigma}54-RNA polymerase and appears to drive events that precede DNA opening. Clear evidence for a DNA-interacting activity in the AAA+ domain of PspF was obtained, suggesting that PspF may make a direct contact to the DNA component of a basal promoter complex to promote changes in {sigma}54-RNA polymerase–DNA interactions that favour open complex formation. We also provide evidence for two distinct closed promoter complexes with differing stabilities.


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
J. Schumacher, N. Joly, M. Rappas, D. Bradley, S. R. Wigneshweraraj, X. Zhang, and M. Buck
Sensor I Threonine of the AAA+ ATPase Transcriptional Activator PspF Is Involved in Coupling Nucleotide Triphosphate Hydrolysis to the Restructuring of {sigma}54-RNA Polymerase
J. Biol. Chem., March 30, 2007; 282(13): 9825 - 9833.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Joly, J. Schumacher, and M. Buck
Heterogeneous Nucleotide Occupancy Stimulates Functionality of Phage Shock Protein F, an AAA+ Transcriptional Activator
J. Biol. Chem., November 17, 2006; 281(46): 34997 - 35007.
[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.