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Title: DNA sequence recognition protein associated with a multiprotein form of DNA polymerase alpha

Journal Article · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:5127415

The majority of DNA polymerase ..cap alpha.. activity in HeLa cells has been isolated and purified as a multiprotein Mr 640,000 form. A number of accessory activities cofractionate with this form of polymerase ..cap alpha... Among these are: Cl, C2 primer recognition proteins, primase, a 5' ..-->.. 3' exonuclease, and a 5',5''',P/sup 1/,P/sup 4/-diadenosine tetraphosphate (Ap/sub 4/A) binding protein. Preliminary results suggest an additional factor(s) or protein(s) is present in the multiprotein form of the HeLa cell DNA polymerase ..cap alpha.. which has an affinity for DNA sequences rich in A and T residues. Affinity chromatography on poly(dA)-or oligo(dT)-cellulose yields a highly purified protein. This protein has the ability to bind /sup 3/H-poly (dA) and /sup 3/H-poly(dT) in a nitrocellulose filter binding assay. The further physical properties of this protein and its DNA sequence binding specificity will be discussed.

Research Organization:
Worcester Foundation for Experimental Biology, Shrewsbury, MA
OSTI ID:
5127415
Report Number(s):
CONF-8606151-; TRN: 86-034800
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 45:6; Conference: 76. annual meeting of the Federation of American Society for Experimental Biology, Washington, DC, USA, 8 Jun 1986
Country of Publication:
United States
Language:
English