Probing the ATP-binding site of P1 ParA: partition and repression have different requirements for ATP binding and hydrolysis.

ABSTRACT: The ParA family of proteins is involved in partition of a variety of plasmid and bacterial chromosomes. P1 ParA plays two roles in partition: it acts as a repressor of the par operon and has an undefined yet indispensable role in P1 plasmid localization. We constructed seven mutations in three putative ATP-binding motifs of ParA. Three classes of phenotypes resulted, each represented by mutations in more than one motif. Three mutations created 'super-repressors', in which repressor activity was much stronger than in wild-type ParA, while the remainder damaged repressor activity. All mutations eliminated partition activities, but two showed a plasmid stability defect that was worse than that of a null mutation. Four mutant ParAs, two super-repressors and two weak repressors, were analyzed b

SUBMITTER: Fung E 

PROVIDER: S-EPMC125607 | biostudies-literature | 2001 Sep

REPOSITORIES: biostudies-literature