Nucleic Acids Research, Vol 27, Issue 20 4106-4113, Copyright © 1999 by Oxford University Press
HJ Ball, A Melnick, R Shaknovich, RA Kohanski and JD Licht
A binding site selection from a CpG island library for the promyelocytic
leukemia zinc finger protein (PLZF) identified two high affinity PLZF
binding sites. These sequences also bound RARalpha/PLZF, a fusion protein
formed in chromosomal translocation t(11;17)(q23;q21) associated with acute
promyelocytic leukemia. PLZF bound DNA as a slowly migrating complex with
an estimated mol. wt of 600 kDa whose formation was dependent on the
POZ/dimerization domain of PLZF. The PLZF-DNA complex was unable to form in
the presence of cdc2 antibodies. A PLZF-cdc2 interaction was further
demonstrated by co- immunoprecipitation and a biotin-streptavidin pull-down
assay. PLZF is a phosphoprotein and immunoprecipi-tates with a cdc2-like
kinase activity. The PLZF-DNA complex was abolished with the addition of a
phosphatase. These studies suggest that the activity of PLZF, a regulator
of the cell cycle, may be modulated by cell cycle proteins. RARalpha/PLZF
did not complex with cdc2, this potentially contributing to its aberrant
transcriptional properties and potential role in leukemo-genesis.
ARTICLES
The promyelocytic leukemia zinc finger (PLZF) protein binds DNA in a high molecular weight complex associated with cdc2 kinase
Derald H. Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York, NY 10029, USA.
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