Stereochemical course of nucleotidyl transfer catalyzed by bacteriophage T7 induced DNA polymerase.

Published

Journal Article

The bacteriophage T7 induced DNA polymerase, consisting of the phage specified gene 5 protein associated with Escherichia coli thioredoxin, catalyzes the copolymerization of SP-dATP alpha S with dTTP, producing the alternating of polymer poly[dTs-A)] by a mechanism involving inversion of configuration at P alpha. Degradation of poly[d(5s-A)] by the nucleolytic action of E. coli DNA polymerase produced the dinucleotide pdTps-dA, whose configuration at the phosphorothioate diester was assigned as R by comparison of the phosphorus-31 nuclear magnetic resonance chemical shift (55.0 ppm downfield from H3PO4) with that of an authentic sample. Further degradation by alkaline phosphatase to Rp-dTps-dA (55.6 ppm downfield from H3PO4) confirmed the configuration. The stereochemistry provides no evidence of a double displacement mechanism.

Full Text

Duke Authors

Cited Authors

  • Brody, RS; Adler, S; Modrich, P; Stec, WJ; Leznikowski, ZJ; Frey, PA

Published Date

  • May 11, 1982

Published In

Volume / Issue

  • 21 / 10

Start / End Page

  • 2570 - 2572

PubMed ID

  • 7093204

Pubmed Central ID

  • 7093204

International Standard Serial Number (ISSN)

  • 0006-2960

Language

  • eng

Conference Location

  • United States