Skip Navigation



Nucleic Acids Research Advance Access published online on May 23, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn269
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (5828K) Freely available
Right arrow Screen PDF (739K) Freely available
Right arrow Supplementary Data
Right arrowOA All Versions of this Article:
36/12/3879    most recent
gkn269v1
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 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 Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Rowley, P. A.
Right arrow Articles by Smith, M. C. M.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rowley, P. A.
Right arrow Articles by Smith, M. C. M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

A motif in the C-terminal domain of {phi}C31 integrase controls the directionality of recombination

Paul A. Rowley1, Matthew C. A. Smith2, Ellen Younger1 and Margaret C. M. Smith1,*

1Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB252ZD and 2Institute of Genetics, University of Nottingham, Nottingham NG7 2UH, UK

*To whom correspondence should be addressed. Tel: +44 1224 555739; Fax: +44 1224 555844; Email: maggie.smith{at}abdn.ac.uk

Received March 1, 2008. Revised March 12, 2008. Accepted April 22, 2008.

Bacteriophage {phi}C31 encodes an integrase, which acts on the phage and host attachment sites, attP and attB, to form an integrated prophage flanked by attL and attR. In the absence of accessory factors, {phi}C31 integrase cannot catalyse attL x attR recombination to excise the prophage. To understand the mechanism of directionality, mutant integrases were characterized that were active in excision. A hyperactive integrase, Int E449K, gained the ability to catalyse attL x attR, attL x attL and attR x attR recombination whilst retaining the ability to recombine attP x attB. A catalytically defective derivative of this mutant, Int S12A, E449K, could form stable complexes with attP/attB, attL/attR, attL/attL and attR/attR under conditions where Int S12A only complexed with attP/attB. Further analysis of the Int E449K-attL/attR synaptic events revealed a preference for one of the two predicted synapse structures with different orientations of the attL/attR sites. Several amino acid substitutions conferring hyperactivity, including E449K, were localized to one face of a predicted coiled-coil motif in the C-terminal domain. This work shows that a motif in the C-terminal domain of {phi}C31 integrase controls the formation of the synaptic interface in both integration and excision, possibly through a direct role in protein–protein interactions.


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. Bacteriol.Home page
P. A. Rowley and M. C. M. Smith
Role of the N-Terminal Domain of {phi}C31 Integrase in attB-attP Synapsis
J. Bacteriol., October 15, 2008; 190(20): 6918 - 6921.
[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.