D. Ferbus et al., IDENTIFICATION, NUCLEAR-LOCALIZATION, AND BINDING ACTIVITIES OF OZF -A HUMAN PROTEIN SOLELY COMPOSED OF ZINC-FINGER MOTIFS, European journal of biochemistry, 236(3), 1996, pp. 991-995
The OZF cDNA was identified in a human mammary cell line and encodes a
polypeptide solely composed of ten zinc-finger motifs which belongs t
o the Kruppel family of zinc-finger proteins. The OZF protein produced
in Escherichia coli binds zinc ions, DNA and heparin. These binding a
ctivities are characteristic of zinc-finger proteins. Immunochemical a
nalysis using antibodies produced against the recombinant protein dete
cted its expression in human mammary epithelial cells but not in strom
a cells, which is consistent with the pattern of expression observed a
t the RNA level in cell cultures. Western blot analysis demonstrated t
he expression of a 33-kDa nuclear protein similar in size to the predi
cted protein and therefore excluded the presence of an additional tran
s-acting domain. These data establish the unique structure of the OZF
protein which is distinct from previously identified zinc-finger prote
ins. In addition, OZF protein overexpression was found in a tumor cell
line, which suggests a possible involvement in carcinogenesis.