Protein kinase C β from Friend erythroleukemia cells is associated with chromatin and DNA

Certain protein kinase C (PKC) isotypes are localized to the nucleus during cellular proliferation in murine erythroid cells, as well as in human promyelocytic leukemia and erythroleukemia cells. Because the structure of these PKC isotypes contains a conserved cysteine-rich region that contains the zinc finger DNA binding motif, we tested the hypothesis that selected PKC isotypes found in Friend erythroleukemia cells can bind to DNA. Cell lysates from murine Friend erythroleukemia cells, which express α, βI, and βII PKC, expressed greater amounts of the β isoforms than the α isoform of PKC in their nuclei, and PKC βI was found in the chromatin of these cells. Lysates of these cells were tested for their ability to bind to a DNA-cellulose columm. Bound proteins were eluted with a step gradient of increasing KCl concentrations, and eluant fractions were then subjected to immunoblot analysis using isotype-specific antibodies to the α and βI isotypes of PKC. DNA binding was detected for the PKC βI isotype, which is present in the nucleus, but not for the more abundant PKC α isotype, which resides primarily in the cytoplasm. These results demonstrate that PKC can associate with DNA, and that this association is isotype specific in Friend erythroleukemia cells. (Mol Cell Biochem 151: 107-111, 1995)