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B or PU.1 to Mediate IL-4-Induced Activation of IgE Germline Gene Transcription
Department of Immunology, Novartis Research Institute, Vienna, Austria
Ig heavy chain class switching to IgE is directed by IL-4 and IL-13
by inducing transcription from the IgE germline promoter. A crucial
transcription factor in this process is STAT6, which binds to a
specific DNA element upon cytokine activation. In this paper it is
shown that the B cell- and monocyte-specific factor PU.1 interacts with
a closely spaced sequence in the human IgE germline promoter that
overlaps with a previously described binding site for
NF
B/rel. The authenticity of PU.1 was demonstrated by
specific competition and supershifts in EMSA experiments. In addition,
in vitro translated PU.1 could interact with an oligonucleotide derived
from the IgE germline promoter containing the PU.1 binding site and
migrated with the same mobility compared with the complex formed with
nuclear extracts. Transient transfection experiments using IgE germline
promoter reporter gene constructs demonstrated that mutations affecting
DNA binding of PU.1 or NFB/rel had no or little
effect on IL-4 inducibility of these plasmids. However, point mutations
that abolished binding of both factors abrogated cytokine inducibility.
No strict spacing of the STAT6 and the composite PU.1/NF-B elements
is required for IL-4 induction. IL-4-induced STAT6 DNA binding was
retained in PU.1-/NFB/rel-
double mutants. The data demonstrate that cooperation of STAT6 with at
least PU.1 or NFB/rel is necessary for IL-4-induced
activation of IgE germline gene transcription.
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