Abstract
DNA polymerase has been isolated from the cytoplasm of several mammalian tissues as well as several cell lines in culture1–8. This has been puzzling because DNA replication and repair are processes generally believed to be restricted to the nucleus, where chromatin is located. It has been suggested that cytoplasmic DNA polymerase is newly synthesised, not yet having been transported to the nucleus9 or that it could have leaked from the nucleus during cell disruption10,11. Investigation of possible functions of a DNA polymerase in the cytoplasm have been inhibited by the possibility that the cytoplasmic location of this enzyme is either artefactual or trivial. To demonstrate that this is not so, we have investigated the presence of the enzyme in the reticulocyte, which is an anucleate cell. We wish to report here the purification and characterisation of a DNA polymerase from rabbit reticulocytes, and compare its properties with those of the DNA polymerase purified from the cytoplasm of immature erythroblasts of bone marrow, the precursor of the reticulocyte.
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BYRNES, J., DOWNEY, K., JURMARK, B. et al. Reticulocyte DNA polymerase. Nature 248, 687–690 (1974). https://doi.org/10.1038/248687a0
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DOI: https://doi.org/10.1038/248687a0
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