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Journal of Bacteriology, March 2000, p. 1541-1548, Vol. 182, No. 6
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
TraG from RP4 and TraG and VirD4 from Ti Plasmids
Confer Relaxosome Specificity to the Conjugal Transfer System of
pTiC58
Claire M.
Hamilton,1,
Hyewon
Lee,2
Pei-Li
Li,1
David M.
Cook,1,
Kevin R.
Piper,3
Susanne Beck
von Bodman,1,§
Erich
Lanka,4
Walt
Ream,2 and
Stephen K.
Farrand1,3,*
Departments of Crop
Sciences1 and
Microbiology,3 University of Illinois at
Urbana-Champaign, Urbana, Illinois 61801; Department of
Microbiology, Oregon State University, Corvallis, Oregon
973312; and Max-Planck-Institut
für Molekulare Genetik, Dahlem, D-14195 Berlin,
Germany4
Received 26 August 1999/Accepted 21 December 1999
Plasmid conjugation systems are composed of two components, the DNA
transfer and replication system, or Dtr, and the mating pair formation
system, or Mpf. During conjugal transfer an essential factor, called
the coupling protein, is thought to interface the Dtr, in the form of
the relaxosome, with the Mpf, in the form of the mating bridge. These
proteins, such as TraG from the IncP1 plasmid RP4 (TraGRP4)
and TraG and VirD4 from the conjugal transfer and T-DNA transfer
systems of Ti plasmids, are believed to dictate specificity of the
interactions that can occur between different Dtr and Mpf components.
The Ti plasmids of Agrobacterium tumefaciens do not
mobilize vectors containing the oriT of RP4, but these IncP1 plasmid derivatives lack the trans-acting Dtr
functions and TraGRP4. A. tumefaciens
donors transferred a chimeric plasmid that contains the
oriT and Dtr genes of RP4 and the Mpf genes of pTiC58,
indicating that the Ti plasmid mating bridge can interact with the RP4
relaxosome. However, the Ti plasmid did not mobilize transfer from an
IncQ relaxosome. The Ti plasmid did mobilize such plasmids if
TraGRP4 was expressed in the donors. Mutations in
traGRP4 with defined effects on the RP4
transfer system exhibited similar phenotypes for Ti plasmid-mediated
mobilization of the IncQ vector. When provided with VirD4, the
tra system of pTiC58 mobilized plasmids from the IncQ
relaxosome. However, neither TraGRP4 nor VirD4 restored
transfer to a traG mutant of the Ti plasmid. VirD4 also
failed to complement a traGRP4 mutant for transfer from the RP4 relaxosome or for RP4-mediated mobilization from
the IncQ relaxosome. TraGRP4-mediated mobilization of the IncQ plasmid by pTiC58 did not inhibit Ti plasmid transfer, suggesting that the relaxosomes of the two plasmids do not compete for the same
mating bridge. We conclude that TraGRP4 and VirD4 couples the IncQ but not the Ti plasmid relaxosome to the Ti plasmid mating bridge. However, VirD4 cannot couple the IncP1 or the IncQ relaxosome to the RP4 mating bridge. These results support a model in which the
coupling proteins specify the interactions between Dtr and Mpf
components of mating systems.
*
Corresponding author. Mailing address: Department of
Crop Sciences, University of Illinois at Urbana-Champaign, 240 Edward R. Madigan Laboratory (ERML), 1201 West Gregory Dr., Urbana, IL 61801. Phone: (217) 333-1524. Fax: (217) 244-7830. E-mail:
stephenf{at}uiuc.edu.

Present address: Clontech, Inc., Palo Alto, CA
94303.

Present address: MJ Research, Inc., Indian Village, NV
89451.
§
Present address: Department of Plant Science, University of
Connecticut, Storrs, CT
06269.
Journal of Bacteriology, March 2000, p. 1541-1548, Vol. 182, No. 6
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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