Nucleic Acids Research, Vol 25, Issue 6 1108-1116, Copyright © 1997 by Oxford University Press
J Kaplan and K Calame
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.
ARTICLES
The ZiN/POZ domain of ZF5 is required for both transcriptional activation and repression
Department of Microbiology, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.
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