Evidence for template-specific sites in DNA polymerases

Stuart L. Marcus, Mukund Modak, Liebe F. Cavalieri

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Using rabbit hemoglobin messenger RNA as template, E. coli polymerase I produces poly (dT), poly (dA)·(dT) and antimessenger DNA products. Mild heating of the enzyme causes a differential loss in activity as indicated by three rates of inactivation for the three types of synthesis. Heat inactivation studies have also been carried out with DNA polymerases from oncogenic RNA viruses and mammalian sources using various homopolymer-oligomer pairs as primertemplates. In general, for any given enzyme these synthetic primer-templates reveal different extents of inactivation of the polymerase. These findings may be interpreted to suggest a) that the binding of DNA polymerase to various primer-templates produces conformational changes in the enzyme which are dependent on the type of template bound, or b) that many, if not all, DNA polymerases have different subsites for different templates.

Original languageEnglish (US)
Pages (from-to)516-521
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume56
Issue number2
DOIs
StatePublished - Jan 23 1974
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

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