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Journal of Bacteriology, October 2008, p. 6918-6921, Vol. 190, No. 20
0021-9193/08/$08.00+0     doi:10.1128/JB.00612-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Role of the N-Terminal Domain of {phi}C31 Integrase in attB-attP Synapsis{triangledown}

Paul A. Rowley{dagger} and Margaret C. M. Smith*

Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom

Received 2 May 2008/ Accepted 1 August 2008

{phi}C31 integrase is a serine recombinase containing an N-terminal domain (NTD) that provides catalytic activity and a large C-terminal domain that controls which pair of DNA substrates is able to synapse. We show here that substitutions in amino acid V129 in the NTD can lead to defects in synapsis and DNA cleavage, indicating that the NTD also has an important role in synapsis.

* Corresponding author. Mailing address: Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom. Phone: 44 1224 555739. Fax: 44 1224 555844. E-mail: maggie.smith{at}abdn.ac.uk

{triangledown} Published ahead of print on 8 August 2008.

{dagger} Present address: University of Texas at Austin, Molecular Genetics and Microbiology, 1 University Station A5000, Austin, TX 78712-0162.

Journal of Bacteriology, October 2008, p. 6918-6921, Vol. 190, No. 20
0021-9193/08/$08.00+0     doi:10.1128/JB.00612-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • McEwan, A. R., Rowley, P. A., Smith, M. C. M. (2009). DNA binding and synapsis by the large C-terminal domain of {phi}C31 integrase. Nucleic Acids Res 37: 4764-4773 [Abstract] [Full Text]  


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