Open AccessElongation of primed DNA templates by eukaryotic DNA polymerases.
Author(s) -
JohE Ikeda,
Mathew Longiaru,
Marshall S. Horwitz,
Jerard Hurwitz
Publication year - 1980
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.10.5827
Subject(s) - dna polymerase , dna clamp , dna polymerase ii , primer (cosmetics) , polymerase , microbiology and biotechnology , primase , dna polymerase i , biology , dna , dna polymerase mu , dna synthesis , dna polymerase delta , biochemistry , chemistry , rna , circular bacterial chromosome , reverse transcriptase , gene , organic chemistry
The combined action of DNA polymerase alpha and DNA polymerase beta leads to the synthesis of full-length linear DNA strands with phi X174 DNA templates containing an RNA primer. The reaction can be carried out in two stages. In the first stage, DNA polymerase alpha catalyzes the synthesis of a chain that averaged 230 deoxynucleotides long and was covalently linked to the RNA primer. In the second stage, DNA polymerase beta elongates the DNA strand covalently attached to the RNA primer to full length. With DNA primers, DNA polymerase alpha catalyzes only limited deoxynucleotide addition whereas DNA polymerase beta alone elongates DNA primed templates to full length. DNA polymerase beta can also stimulate the synthesis of adenovirus DNA in vitro in the presence of a cytosol extract from adenovirus-infected cells. In all of these systems, dNMP incorporation catalyzed by DNA polymerase beta was sensitive to N-ethylmaleimide; however, this polymerase activity was resistant to N-ethylmaleimide with poly(rA) x (dT) as the primer template.