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Journal of Bacteriology, April 1999, p. 2124-2131, Vol. 181, No. 7
Department of Microbiology and Institute for
Cellular and Molecular Biology, University of Texas, Austin, Texas
78712
Received 28 October 1998/Accepted 19 January 1999
MobB is a small protein encoded by the broad-host-range plasmid
R1162 and required for efficient mobilization of its DNA during conjugation. The protein was shown previously to stabilize the relaxosome, the complex of plasmid DNA and mobilization proteins at the
origin of transfer (oriT). We have generated in-frame
mobB deletions that specifically inactivate the stabilizing
effect of MobB while still allowing a high rate of transfer. Thus, MobB has two genetically distinct functions in transfer. The effect of
another deletion, extending into mobA, indicates that both functions require a specific region of MobA protein that is distinct from the nicking-ligating domain. The mobB mutations that
specifically affected stability also resulted in poor growth of cells,
due to increased transcription from the promoters adjacent to
oriT. The effects of the mutations could be suppressed not
only by full-length MobB provided in trans, as expected,
but also by additional copies of oriT, cloned in pBR322. In
addition, in the presence of MobA both the full-length and truncated
forms of MobB stimulated recombination between
oriT-containing plasmids. We propose a model in which MobB
regulates expression of plasmid genes by altering the stability of the
relaxosome, in a manner that involves the coupling of plasmid molecules.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Stabilization of the Relaxosome and Stimulation of
Conjugal Transfer Are Genetically Distinct Functions of the R1162
Protein MobB
*
Corresponding author. Mailing address: Department of
Microbiology and Institute for Cellular and Molecular Biology,
University of Texas, Austin, TX 78712. Phone: (512) 471-3817. Fax:
(512) 471-7088. E-mail: rmeyer{at}mail.utexas.edu.
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