title: Biochemical activities of the parA partition protein of the P1 plasmid.
abstract: The unit-copy P1 plasmid depends for stability on a plasmid-encoded partition region called par, consisting of the parA and parB genes and the parS site. ParA is absolutely required for partition, but its partition-critical role is not known. Purified ParA protein is shown to possess an ATPase activity in vitro which is specifically stimulated by purified ParB protein and by DNA. ParA is responsible for regulation of expression of parA and parB, and purified ParA has an ATP-dependent, site-specific DNA binding activity which recognizes a sequence that overlaps the parA promoter. The role of the ATP-dependence of the binding activity, as well as other possible functions of the ATPase activity in partition, is discussed.
authors.affiliation: ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, Maryland 21702-1201.
authors.forename: M A
authors.initials: MA
authors.lastname: Davis
authors.forename: K A
authors.initials: KA
authors.lastname: Martin
authors.forename: S J
authors.initials: SJ
authors.lastname: Austin
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D008969:Molecular Sequence Data; D010957:Plasmids
chemical_list: D001426:Bacterial Proteins; C052883:chromosome partition proteins, bacterial; D000255:Adenosine Triphosphate; D004247:DNA; D000251:Adenosine Triphosphatases