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Nucleic Acids Research, 1990, Vol. 18, No. 22 6659-6663
© 1990

ENZYMOLOGY

Purification and characterization of a DNA polymerase from the cyanobacterium Anacystis nidulans R2

Hsiu-Jin Lin, Gordon C. Cannon and Sabine Heinhorst*

Department of Chemistry and Biochemistry, University of Southern Mississippi Southern Station Box 5043, Hattiesburg, MS 39406, USA

*To whom correspondence should be addressed

Received May 31, 1990. Revised September 14, 1990. Accepted September 14, 1990.

A DNA polymerase has been highly purified from Anacystis nidulans R2. Electrophoretic analysis in sodium dodecyl sulfate-polyacrylamide gels revealed that the final fraction contains three bands of Mr 107,000, 93,000, and 51,000, respectively. Analysis of purified DNA polymerase activity in situ indicates that of the three polypeptides the Mr 107,000 species has the catalytic activities. The native molecular weight of the enzyme was estimated by glycerol gradient sedimentation to be 100,000. The enzyme has an absolute requirement for a divalent cation. Mg2+ can be replaced with Mn2+, but the DNA polymerase is less active. Potassium chloride stimulates the enzyme, while potassium phosphate has no apparent effect. The enzyme is active over a pH range from 7.5 to 9.5 in 50mM Tris-HCI buffer. The ability of the cyanobacterial DNA polymerase to use activated DNA as a template, Its associated 3' ->5' and 5'->3' exonuclease activities, as well as its resistance to N-ethylmaleimide, dideoxynucleotides, arabinosyl-CTP and aphidicolln suggest a similarity between this enzyme and E. coli DNA polymerase I. This is the first characterization of a DNA polymerase from a cyanobacterium.


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