ASSOCIATION OF DIADENOSINE 5',5'''-P1,P4-TETRAPHOSPHATE BINDING-PROTEIN WITH HELA-CELL DNA POLYMERASE-ALPHA

  • 1 January 1981
    • journal article
    • research article
    • Vol. 256  (23) , 2148-2151
Abstract
An electrophoretically homogeneous high MW form (640,000) of [human cervical carcinoma] HeLa cell DNA polymerase .alpha. catalyzed 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 covalently attached to the 5''-end of the poly(dA) product. An Ap4A binding protein is tightly associated with the high MW 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.