Nucleic Acids Research, Vol 25, Issue 24 4915-4920, Copyright © 1997 by Oxford University Press
N Liu, FC Lucibello, K Korner, LA Wolfraim, J Zwicker and R Muller
The cdc25C , cdc2 and cyclin A promoters are controlled by transcriptional
repression through two contiguous protein binding sites, termed the CDE and
CHR. In the present study we have identified a factor, CDF-1, which
interacts with the cdc25C CDE-CHR module. CDF-1 binds to the CDE in the
major groove and to the CHR in the minor grove in a cooperative fashion in
vitro , in a manner similar to that seen by genomic footprinting. In
agreement with in vivo binding data and its putative function as a periodic
repressor, DNA binding by CDF-1 in nuclear extracts is down-regulated
during cell cycle progression. CDF-1 also binds avidly to the CDE-CHR
modules of the cdc2 and cyclin A promoters, but not to the E2F site in the
B- myb promoter. Conversely, E2F complexes do not recognize the cdc25C
CDE-CHR and CDF-1 is immunologically unrelated to all known E2F and DP
family members. This indicates that E2F- and CDF-mediated repression is
controlled by different factors acting at different stages during the cell
cycle. While E2F-mediated repression seems to be associated with genes that
are up-regulated early (around mid G1), such as B- myb , CDE-CHR-
controlled genes, such as cdc25C , cdc2 and cyclin A , become derepressed
later. Finally, the fractionation of native nuclear extracts on glycerol
gradients leads to separation of CDF-1 from both E2F complexes and pocket
proteins of the pRb family. This emphasizes the conclusion that CDF-1 is
not an E2F family member and points to profound differences in the cell
cycle regulation of CDF-1 and E2F.
ARTICLES
CDF-1, a novel E2F-unrelated factor, interacts with cell cycle- regulated repressor elements in multiple promoters
Institut fur Molekularbiologie und Tumorforschung (IMT), Philipps- Universitat Marburg Emil-Mannkopff-Strasse 2, D-35033 Marburg, Germany.
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