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Journal of Bacteriology, April 2000, p. 1889-1894, Vol. 182, No. 7
Laboratory of Biochemistry, National Cancer
Institute, Bethesda, Maryland 20892-4255
Received 20 September 1999/Accepted 7 January 2000
Partition cassettes, essential for the segregational stability of
low-copy-number bacterial plasmids, typically encode two autoregulated
proteins and an adjacent cis-acting centromere analog to
which one or perhaps both proteins bind. The diminutive partition region of pTAR of Agrobacterium spp. was reported to be
exceptional, encoding only a single protein, ParA (D. R. Gallie
and C. I. Kado, J. Mol. Biol. 193:465-478, 1987). However,
resequencing of the region revealed two small downstream genes,
parB and orf-84, of which only parB
was found to be essential for partitioning in A. tumefaciens. Purified ParA exhibited a weak ATPase activity that
was modestly increased by nonspecific DNA. ParB bound in vitro to
repeated sequences present in a region, parS, that
possesses centromere and operator functions and within which we
identified the primary transcription start site by primer extension. In
certain respects the Par proteins behave normally in the foreign host Escherichia coli. In E. coli, as in A. tumefaciens, ParB repressed the partition operon; ParA, inactive
alone, augmented this repression. Functional similarities between the
partition system of pTAR and those of other plasmids and bacteria are
prominent, despite differences in size, organization, and amino acid sequence.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
pTAR-Encoded Proteins in Plasmid
Partitioning

and
*
Corresponding author. Mailing address: Laboratory of
Biochemistry, National Cancer Institute, National Institutes of Health, 37 Convent Dr., Bethesda, MD 20892-4255. Phone: (301) 496-5226. Fax:
(301) 402-3095. E-mail: myarmo{at}helix.nih.gov.
Present address: Oral Infection and Immunity Branch, National
Institute of Dental and Craniofacial Research, National Institutes of
Health, Bethesda, MD 20892.
Present address: Laboratory of Genetics and Physiology, National
Institute of Diabetes and Digestive and Kidney Diseases, National
Institutes of Health, Bethesda, MD 20892.
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