DNA polymerase III accessory proteins. IV. Characterization of chi and psi

J Biol Chem. 1993 Jun 5;268(16):11779-84.

Abstract

The gamma complex (gamma delta delta' chi psi) subassembly of the Escherichia coli replicase initiates processive replication upon assembling the ring-shaped beta subunit around DNA. The beta ring acts as a clamp to hold the replicase down to DNA for highly processive synthesis. In this report we characterize the chi and psi subunits of the gamma complex. Both chi and psi are monomeric, and they associate to form a 1:1 complex. The chi subunit does not form a complex with gamma, but psi binds gamma tightly thereby acting as a bridge to assimilate chi into the gamma complex structure. The psi subunit stimulated the ATPase and replication activities of gamma. The chi subunit only stimulated the activities of gamma when the psi subunit was also present thus reflecting the structure where psi bridges the interaction of chi with gamma.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Chromatography, Gel
  • DNA Helicases*
  • DNA Polymerase III / isolation & purification
  • DNA Polymerase III / metabolism*
  • DNA Replication*
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / enzymology*
  • Kinetics
  • Macromolecular Substances
  • Molecular Weight
  • Protein Conformation

Substances

  • Macromolecular Substances
  • DNA Polymerase III
  • Adenosine Triphosphatases
  • DNA Helicases