Association of diadenosine 5',5"'-P1,P4-tetraphosphate binding protein with HeLa cell DNA polymerase alpha

J Biol Chem. 1981 Dec 10;256(23):12148-51.


An electrophoretically homogeneous high molecular weight form (640,000) of HeLa cell DNA polymerase alpha was shown to catalyze DNA synthesis with a variety of di- and oligoriboadenylates and oligodeoxyriboadenylates as primers with poly(dT) as template. Diadenosine 5',5"'-P1,p4-tetraphosphate (Ap4A) can be utilized as a primer with poly(dT) as template and was found to be covalently attached to the 5'-end of the poly(dA) product. An Ap4A binding protein is tightly associated with the high molecular weight form of DNA polymerase alpha. This protein which exhibits high affinity, noncovalent binding of Ap4A is resolved from the multiprotein DNA polymerase alpha complex, along with other accessory proteins, by hydrophobic affinity chromatography on phenyl-Sepharose columns.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenine Nucleotides / metabolism*
  • Carrier Proteins / metabolism*
  • Chromatography, Affinity
  • DNA Polymerase II / isolation & purification
  • DNA Polymerase II / metabolism*
  • DNA Replication
  • DNA-Directed DNA Polymerase / metabolism*
  • Dinucleoside Phosphates*
  • HeLa Cells / metabolism
  • Humans
  • Macromolecular Substances
  • Multiprotein Complexes
  • Tryptophan-tRNA Ligase / metabolism


  • AP4A binding protein, human
  • Adenine Nucleotides
  • Carrier Proteins
  • Dinucleoside Phosphates
  • Macromolecular Substances
  • Multiprotein Complexes
  • diadenosine tetraphosphate
  • DNA Polymerase II
  • DNA-Directed DNA Polymerase
  • Tryptophan-tRNA Ligase