title: pTAR-encoded proteins in plasmid partitioning.
abstract: 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.
authors.affiliation: Laboratory of Biochemistry, National Cancer Institute, Bethesda, Maryland 20892-4255, USA.
authors.forename: K
authors.initials: K
authors.lastname: Kalnin
authors.forename: S
authors.initials: S
authors.lastname: Stegalkina
authors.forename: M
authors.initials: M
authors.lastname: Yarmolinsky
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D001483:Base Sequence; D002503:Centromere / Q000235:genetics / Q000378:metabolism; D004269:DNA, Bacterial / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D004789:Enzyme Activation; D004926:Escherichia coli / Q000235:genetics; D019143:Evolution, Molecular; D020868:Gene Silencing; D005798:Genes, Bacterial / Q000235:genetics* / Q000502:physiology; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics / Q000502:physiology; D009876:Operon / Q000235:genetics; D010957:Plasmids / Q000235:genetics*; D011401:Promoter Regions, Genetic / Q000235:genetics; D012329:RNA, Bacterial / Q000032:analysis / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D012231:Rhizobium / Q000201:enzymology / Q000235:genetics*; D014158:Transcription, Genetic / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D012329:RNA, Bacterial; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; C052883:chromosome partition proteins, bacterial; D000251:Adenosine Triphosphatases