Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (135K) 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 (19)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Mahdi, A. A.
Right arrow Articles by Lloyd, R. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mahdi, A. A.
Right arrow Articles by Lloyd, R. G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, Vol 25, Issue 19 3875-3880, Copyright © 1997 by Oxford University Press

ARTICLES

DNA binding and helicase domains of the Escherichia coli recombination protein RecG

AA Mahdi, P McGlynn, SD Levett and RG Lloyd
Department of Genetics, University of Nottingham, Queens Medical Centre, Nottingham NG7 2UH, UK.

The Escherichia coli RecG protein is a unique junction-specific helicase involved in DNA repair and recombination. The C-terminus of RecG contains motifs conserved throughout a wide range of DNA and RNA helicases and it is thought that this C-terminal half of RecG contains the helicase active site. However, the regions of RecG which confer junction DNA specificity are unknown. To begin to assign structure- function relationships within RecG, a series of N- and C-terminal deletions have been engineered into the protein, together with an N- terminal histidine tag fusion peptide for purification purposes. Junction DNA binding, unwinding and ATP hydrolysis were disrupted by mutagenesis of the N-terminus. In contrast, C-terminal deletions moderately reduced junction DNA binding but almost abolished unwinding. These data suggest that the C-terminus does contain the helicase active site whereas the N-terminus confers junction DNA specificity.
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
 Nucleic Acids ResHome page
A. J. Smith, M. D. Szczelkun, and N. J. Savery
Controlling the motor activity of a transcription-repair coupling factor: autoinhibition and the role of RNA polymerase
Nucleic Acids Res., March 19, 2007; 35(6): 1802 - 1811.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. S. Briggs, A. A. Mahdi, Q. Wen, and R. G. Lloyd
DNA Binding by the Substrate Specificity (Wedge) Domain of RecG Helicase Suggests a Role in Processivity
J. Biol. Chem., April 8, 2005; 280(14): 13921 - 13927.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
J. Kang, D. Tavakoli, A. Tschumi, R. A. Aras, and M. J. Blaser
Effect of Host Species on RecG Phenotypes in Helicobacter pylori and Escherichia coli
J. Bacteriol., November 15, 2004; 186(22): 7704 - 7713.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Tanaka, T. Mizukoshi, C. Taniyama, D. Kohda, K.-i. Arai, and H. Masai
DNA Binding of PriA Protein Requires Cooperation of the N-terminal D-loop/Arrested-fork Binding and C-terminal Helicase Domains
J. Biol. Chem., October 4, 2002; 277(41): 38062 - 38071.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
P. McGlynn, A. A. Mahdi, and R. G. Lloyd
Characterisation of the catalytically active form of RecG helicase
Nucleic Acids Res., June 15, 2000; 28(12): 2324 - 2332.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
G. J. Sharples, S. M. Ingleston, and R. G. Lloyd
Holliday Junction Processing in Bacteria: Insights from the Evolutionary Conservation of RuvABC, RecG, and RusA
J. Bacteriol., September 15, 1999; 181(18): 5543 - 5550.
[Full Text]

Home page
 J. Biol. Chem.Home page
M. C. Whitby and R. G. Lloyd
Targeting Holliday Junctions by the RecG Branch Migration Protein of Escherichia coli
J. Biol. Chem., July 31, 1998; 273(31): 19729 - 19739.
[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.