International Immunology, Vol 9, 1021-1029, Copyright © 1997 by Oxford University Press
L Ma, B Hu and AL Kenter
SNAP, a DNA-binding protein, is specific for the S gamma switch regions.
Two E-2 box consensus binding motifs are located within the SNAP
recognition site. Direct- and competition-binding analyses demonstrate that
a truncated form of the E47 transcription factor, E47S, is capable of
specific interactions with the SNAP binding motif. The methylation
interference pattern for E47S binding on the pl.S gamma 3.A.1 probe was
similar to that previously obtained for SNAP binding activity and was also
related to that found for E47S on the microE5 probe. The interaction of
purified E47S with the SNAP recognition motif was cooperative and formed
complexes which migrated more slowly than the E47S homodimer complex. SNAP
is distinguished from full-length E47 homodimers, found in BCF-1, by its
migration position in the gel shift assay, differences in the
competition-binding results and its unique reactivity with anti-E47
antibodies. SNAP is related to E47 as judged by a similar methylation
interference pattern on S gamma 3 A site DNA and by its reactivity with
anti-E47 mAb. The anti-E47 antibodies block SNAP binding to its cognate
site, whereas anti-E47 antibodies supershift E47 homodimers bound to the
microE5 recognition site. Thus, SNAP may be a hetero-oligomeric species
containing E47 or highly related proteins.
ARTICLES
Ig S gamma-specific DNA binding protein SNAP is related to the helix- loop-helix transcription factor E47
Department of Microbiology and Immunology (M/C 790), University of Illinois College of Medicine, Chicago 60612-7344, USA.
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