Nucleic Acids Research, Vol 26, Issue 7 1681-1688, Copyright © 1998 by Oxford University Press
RJ Rooney, K Rothammer and ER Fernandes
p50E4F is a cellular transcription factor whose DNA binding activity is
stimulated in a phosphorylation-dependent manner by products of the
adenovirus E1A oncogene. Although p50E4F does not contain a bZIP DNA
binding motif, it binds a tandemly repeated palindromic sequence in the
adenovirus E4 promoter that is recognized by a large number of bZIP
proteins, but with much greater stability. Analysis of deletions in the
p50E4F sequence identified the regions that are responsible for its unique
DNA binding properties. Sequence-specific DNA binding and factor
dimerization were localized to a C-terminal region containing two C2H2and
one CCHC zinc finger motifs; the phosphorylation site critical for DNA
binding activity was also localized to this domain. The high stability of
p50E4F binding also required residues within the first 83 amino acids of
the N-terminus. Analysis of single and double amino acid substitutions in
the C-terminal zinc finger domain demonstrated that while the second
C2H2zinc finger was required for DNA binding activity, the putative
structures of the first C2H2and the CCHC zinc fingers were not. Instead,
residues from these other zinc finger motifs appeared to participate in an
alternative structure that mediates DNA binding activity and is regulated
by phosphorylation.
ARTICLES
Mutational analysis of p50E4F suggests that DNA binding activity is mediated through an alternative structure in a zinc finger domain that is regulated by phosphorylation
Department of Biochemistry, St Jude Children's Research Hospital, 332 North Lauderdale, Memphis, TN 38105, USA. robert.rooney@stjude.org
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