Enhancement of the Rate of DNA Polymerase-α Activity on Duplex DNA by a DNA-binding Protein and a DNA-dependent ATPase of Mammalian Cells

  1. F. Cobianchi,
  2. S. Riva,
  3. G. Mastromei*,
  4. S. Spadari,
  5. G. Pedrali-Noy, and
  6. A. Falaschi
  1. Laboratorio di Genetica Biochimica ed Evoluzionistica, C.N.R., and *Istituto di Genetica, Università di Pavia, Pavia, Italy 27100

This extract was created in the absence of an abstract.

Excerpt

The DNA polymerases of animal cells are unable to use completely annealed double-stranded (DS) DNA structures as templates, or in any way to enter a double-strand area adjacent to a single-strand stretch (Weissbach 1977; Falaschi and Spadari 1978). These enzymes (and particularly polymerase α, which is the best known and the most likely to be involved in replicative synthesis) are able to complementarily copy only well-exposed, primed, single-strand stretches in DNA, but are unable to unwind double-strand portions. The same is true also for the bacterial or phage polymerases more directly involved in replicative synthesis, like the polymerase III of Escherichia coli and Bacillus subtilis, the phage T4-induced polymerase, or the T7 polymerase (Kornberg 1974). Study in prokaryote systems has shown that replicative polymerases overcome the problem of handling a DS DNA structure mainly with the help of two types of proteins. The first type of such molecules are the...

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