1996
DOI: 10.1046/j.1365-2958.1996.721423.x
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The P1 ParA protein and its ATPase activity play a direct role in the segregation of plasmid copies to daughter cells

Abstract: The P1 ParA protein is an ATPase that recognizes the parA promoter region where it acts to autoregulate the P1 parA-parB operon. The ParB protein is essential for plasmid partition and recognizes the cis-acting partition site parS. The regulatory role of ParA is also essential because a controlled level of ParB protein is critical for partition. However, we show that this regulatory activity is not the only role for ParA in partition. Efficient partition can be achieved without autoregulation as long as Par pr… Show more

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Cited by 82 publications
(86 citation statements)
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“…Nucleotide binding experiments (Fig. 1) suggest one ATP binding site per ParA monomer, which agrees well with the presence of one putative ATP binding site defined by sequence analysis (10), and the observation that deletion of this region of the protein destroys ATPase activity (7). We have used different adenine nucleotide cofactors to probe the structure and function of ParA.…”
Section: Atp and Adp Binding Bysupporting
confidence: 82%
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“…Nucleotide binding experiments (Fig. 1) suggest one ATP binding site per ParA monomer, which agrees well with the presence of one putative ATP binding site defined by sequence analysis (10), and the observation that deletion of this region of the protein destroys ATPase activity (7). We have used different adenine nucleotide cofactors to probe the structure and function of ParA.…”
Section: Atp and Adp Binding Bysupporting
confidence: 82%
“…(Fig. 1) and hydrolyzes ATP (8), and one or both of these activities are essential for both its regulation and partition activities (7). Nucleotide binding experiments (Fig.…”
Section: Atp and Adp Binding Bymentioning
confidence: 99%
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