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ZF5 is a ubiquitously expressed protein originally identified by its ability to bind and repress the murine c-myc promoter. It contains five C-terminal zinc fingers and a conserved N-terminal ZiN/POZ domain. This motif, found in a growing number of zinc finger proteins, can inhibit DNA binding and mediate dimerization [Bardwell, V.J. and Treisman,R. (1994) Genes Dev., 8,1664-1677]. In the current study, a cyclic amplification and selection of targets (CAST) protocol detected preferred ZF5 binding sites which are highly GC-rich. Binding to these sites by ZF5 depended upon the zinc fingers and was enhanced when the ZiN/POZ domain was removed. Using transient cotransfection assays, ZF5 was shown to activate the HIV-1 LTR and repress the beta-actin promoter. The ZiN/POZ domain was shown to mediate ZF5-dependent transcriptional activation and repression. From these data, we conclude that ZF5 can both activate and repress in the context of different natural promoters and that its ZiN/POZ domain can affect two functions; DNA binding and transcriptional modulation.

The ZiN/POZ domain of ZF5 is required for both transcriptional activation and repression