Soj (ParA) DNA binding is mediated by conserved arginines and is essential for plasmid segregation

Soj is a member of the ParA family of ATPases involved in plasmid and chromosomal segregation. It binds nonspecifically and cooperatively to DNA although the function of this binding is unknown. Here, we show that mutation of conserved arginine residues that map to the surface of Bacillus subtilis S...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2007-12, Vol.104 (51), p.20326-20331
Main Authors: Hester, Christina M, Lutkenhaus, Joe
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Adenosine triphosphatases
Amino Acid Sequence
Arginine - chemistry
Arginine - genetics
Bacillus subtilis
Bacillus subtilis - enzymology
Bacillus subtilis - genetics
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Binding sites
Biological Sciences
Caulobacter crescentus
Cell Nucleus - ultrastructure
Chromosome Segregation - genetics
Chromosomes, Bacterial - genetics
Conserved Sequence
Daughter cells
Deoxyribonucleic acid
Dimerization
Dimers
DNA
DNA, Bacterial - metabolism
E coli
Escherichia coli
F Factor - genetics
Genetic loci
Genetic mutation
Green Fluorescent Proteins - analysis
Green Fluorescent Proteins - genetics
Molecular Sequence Data
Mutation
Plasmids
Polymerization
Proteins
Pseudomonas aeruginosa
Pseudomonas putida
Streptomyces coelicolor
Vibrio cholerae
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Summary:Soj is a member of the ParA family of ATPases involved in plasmid and chromosomal segregation. It binds nonspecifically and cooperatively to DNA although the function of this binding is unknown. Here, we show that mutation of conserved arginine residues that map to the surface of Bacillus subtilis Soj caused only minimal effects on nucleotide-dependent dimerization but had dramatic effects on DNA binding. Using a model plasmid partitioning system in Escherichia coli, we find that Soj DNA-binding mutants are deficient in plasmid segregation. The location of the arginines on the Soj structure explains why DNA binding depends on dimerization and was used to orient the Soj dimer on the DNA, revealing the axis of Soj polymerization. The arginine residues are conserved among other chromosomal homologues, including the ParAs from Caulobacter crescentus, Pseudomonas aeruginosa, Pseudomonas putida, Streptomyces coelicolor, and chromosome I of Vibrio cholerae indicating that DNA binding is a common feature of members of this family.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0705196105