Excess beta subunit can bypass the ATP requirement for highly processive synthesis by the Escherichia coli DNA polymerase III holoenzyme. Journal Article uri icon

Overview

abstract

  • We have previously shown that the processive synthesis of long DNA products on a poly(dA) X oligo(dT)10 primer-template is facilitated by formation of an isolable initiation complex between the Escherichia coli DNA polymerase III holoenzyme and DNA in the presence of ATP (Fay, P. J., Johanson, K. O., McHenry, C. S., and Bambara, R. A. (1982) J. Biol. Chem. 257, 5692-5699). Here we have demonstrated that the ATP requirement for processive synthesis can be obviated by a large excess of the beta subunit of the DNA polymerase III holoenzyme. The reaction which occurs in the presence of excess beta can be distinguished from the ATP-mediated reaction by its salt sensitivity and the lack of stabile initiation complex formation between polymerase and primed DNA. A model is presented which suggest that one of the functions of ATP in the DNA polymerase III holoenzyme reaction is to lock beta into the replicative complex such that it does not readily equilibrate with solution.

publication date

  • September 1, 1983

Date in CU Experts

  • October 1, 2013 12:09 PM

Full Author List

  • Crute JJ; LaDuca RJ; Johanson KO; McHenry CS; Bambara RA

author count

  • 5

citation count

  • 7

Other Profiles

International Standard Serial Number (ISSN)

  • 0021-9258

Electronic International Standard Serial Number (EISSN)

  • 1083-351X

Additional Document Info

start page

  • 11344

end page

  • 11349

volume

  • 258

issue

  • 18