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Journal of Bacteriology, January 2005, p. 697-706, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.697-706.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The F-Plasmid TraI Protein Contains Three Functional Domains Required for Conjugative DNA Strand Transfer

Steven W. Matson1,2,3* and Heather Ragonese1

Department of Biology,1 Curriculum in Genetics & Molecular Biology,2 Program in Molecular & Cellular Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina3

Received 10 August 2004/ Accepted 18 October 2004

The F-plasmid-encoded TraI protein, also known as DNA helicase I, is a bifunctional protein required for conjugative DNA transfer. The enzyme catalyzes two distinct but functionally related reactions required for the DNA processing events associated with conjugation: the site- and strand-specific transesterification (relaxase) reaction that provides the nick required to initiate strand transfer and a processive 5'-to-3' helicase reaction that provides the motive force for strand transfer. Previous studies have identified the relaxase domain, which encompasses the first ~310 amino acids of the protein. The helicase-associated motifs lie between amino acids 990 and 1450. The function of the region between amino acids 310 and 990 and the region from amino acid 1450 to the C-terminal end is unknown. A protein lacking the C-terminal 252 amino acids (TraI{Delta}252) was constructed and shown to have essentially wild-type levels of transesterase and helicase activity. In addition, the protein was capable of a functional interaction with other components of the minimal relaxosome. However, TraI{Delta}252 was not able to support conjugative DNA transfer in genetic complementation experiments. We conclude that TraI{Delta}252 lacks an essential C-terminal domain that is required for DNA transfer. We speculate this domain may be involved in essential protein-protein interactions with other components of the DNA transfer machinery.

* Corresponding author. Mailing address: Department of Biology, CB#3280, Coker Hall, University of North Carolina, Chapel Hill, NC 27599-3280. Phone: (919) 962-0005. Fax: (919) 962-1625. E-mail: smatson{at}bio.unc.edu.

Journal of Bacteriology, January 2005, p. 697-706, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.697-706.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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