Detection of an epitope, not required for polymerization, that is conserved between E.coli DNA polymerases I and III and bacteriophage T4 DNA polymerase. Journal Article uri icon

Overview

abstract

  • Monoclonal antibodies directed against the alpha subunit of the DNA polymerase III holoenzyme (1) of E. coli were tested for cross-reactivity with a variety of polymerases. We found that one monoclonal antibody bound to E. coli DNA polymerase I as well as to DNA polymerase III. A weaker, but specific, interaction was also detected with T4 DNA polymerase. We exploited the proteolysis procedure developed by Setlow, Brutlag and Kornberg (2) to determine which domain of DNA polymerase I contained the conserved epitope. Contrary to expectations, it was not found in the polymerase domain, but in the 5'----3' exonuclease domain. This reveals a sequence or structure, sufficiently important to be conserved among these polymerases, that is not directly involved in the polymerization reaction.

publication date

  • July 1, 1988

Date in CU Experts

  • October 1, 2013 12:09 PM

Full Author List

  • Franden MA; McHenry CS

author count

  • 2

citation count

  • 1

Other Profiles

International Standard Serial Number (ISSN)

  • 0305-1048

Electronic International Standard Serial Number (EISSN)

  • 1362-4962

Additional Document Info

start page

  • 6353

end page

  • 6360

volume

  • 16

issue

  • 14A