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Structural mechanism of ATP-induced polymerization of the partition factor ParF: implications for DNA segregation.

Publication ,  Journal Article
Schumacher, MA; Ye, Q; Barge, MT; Zampini, M; Barillà, D; Hayes, F
Published in: J Biol Chem
July 27, 2012

Segregation of the bacterial multidrug resistance plasmid TP228 requires the centromere-binding protein ParG, the parH centromere, and the Walker box ATPase ParF. The cycling of ParF between ADP- and ATP-bound states drives TP228 partition; ATP binding stimulates ParF polymerization, which is essential for segregation, whereas ADP binding antagonizes polymerization and inhibits DNA partition. The molecular mechanism involved in this adenine nucleotide switch is unclear. Moreover, it is unknown how any Walker box protein polymerizes in an ATP-dependent manner. Here, we describe multiple ParF structures in ADP- and phosphomethylphosphonic acid adenylate ester (AMPPCP)-bound states. ParF-ADP is monomeric but dimerizes when complexed with AMPPCP. Strikingly, in ParF-AMPPCP structures, the dimers interact to create dimer-of-dimer "units" that generate a specific linear filament. Mutation of interface residues prevents both polymerization and DNA segregation in vivo. Thus, these data provide insight into a unique mechanism by which a Walker box protein forms polymers that involves the generation of ATP-induced dimer-of-dimer building blocks.

Duke Scholars

Published In

J Biol Chem

DOI

EISSN

1083-351X

Publication Date

July 27, 2012

Volume

287

Issue

31

Start / End Page

26146 / 26154

Location

United States

Related Subject Headings

  • Protein Structure, Secondary
  • Protein Structure, Quaternary
  • Protein Multimerization
  • Protein Interaction Domains and Motifs
  • Protein Binding
  • Plasmids
  • Molecular Sequence Data
  • Fluorescence Polarization
  • Escherichia coli
  • DNA-Binding Proteins
 

Citation

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Schumacher, M. A., Ye, Q., Barge, M. T., Zampini, M., Barillà, D., & Hayes, F. (2012). Structural mechanism of ATP-induced polymerization of the partition factor ParF: implications for DNA segregation. J Biol Chem, 287(31), 26146–26154. https://doi.org/10.1074/jbc.M112.373696
Schumacher, Maria A., Qiaozhen Ye, Madhuri T. Barge, Massimiliano Zampini, Daniela Barillà, and Finbarr Hayes. “Structural mechanism of ATP-induced polymerization of the partition factor ParF: implications for DNA segregation.J Biol Chem 287, no. 31 (July 27, 2012): 26146–54. https://doi.org/10.1074/jbc.M112.373696.
Schumacher MA, Ye Q, Barge MT, Zampini M, Barillà D, Hayes F. Structural mechanism of ATP-induced polymerization of the partition factor ParF: implications for DNA segregation. J Biol Chem. 2012 Jul 27;287(31):26146–54.
Schumacher, Maria A., et al. “Structural mechanism of ATP-induced polymerization of the partition factor ParF: implications for DNA segregation.J Biol Chem, vol. 287, no. 31, July 2012, pp. 26146–54. Pubmed, doi:10.1074/jbc.M112.373696.
Schumacher MA, Ye Q, Barge MT, Zampini M, Barillà D, Hayes F. Structural mechanism of ATP-induced polymerization of the partition factor ParF: implications for DNA segregation. J Biol Chem. 2012 Jul 27;287(31):26146–26154.

Published In

J Biol Chem

DOI

EISSN

1083-351X

Publication Date

July 27, 2012

Volume

287

Issue

31

Start / End Page

26146 / 26154

Location

United States

Related Subject Headings

  • Protein Structure, Secondary
  • Protein Structure, Quaternary
  • Protein Multimerization
  • Protein Interaction Domains and Motifs
  • Protein Binding
  • Plasmids
  • Molecular Sequence Data
  • Fluorescence Polarization
  • Escherichia coli
  • DNA-Binding Proteins