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Nucleic Acids Research, 1985, Vol. 13, No. 4 1239-1249
© 1985

Articles

Characterization of a 3' -> 5' exonuclease activity in the phage {varphi}29-encoded DNA polymerase

Luis Blanco and Margarita Salas

Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma Canto Blanco, 28049 Madrid, Spain

Received November 22, 1984. Revised January 25, 1985. Accepted January 25, 1985.

Purified protein p2 of phage {varphi}29, characterized as a specific DNA polymerase involved in the initiation and elongation of {varphi}29 DNA replication, contains a 3' -> 5' exonuclease active on single-stranded DNA, but not on double-stranded DNA. No 5'->3' exonuclease activity was found. The 3'->5' exonuclease activity was shown to be associated with the DNA polymerase since 1) the two activities were heat-inactivated with identical kinetics and 2) both activities, present in purified protein p2, cosedimented in a glycerol gradient.


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