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Fig. 3. Cooperative binding of the Drosophila PAX6/2 and SOX2 homologues
to the DC5 sequence in vitro. (A) Schemes of the Drosophila PAX6,
PAX2 and SOX2 homologues and their variants with different molecular tags.
DNA-binding domains are indicated: paired domain (PD), homeodomain (HD),
N-terminal portion of the homeodomain (H) and high mobility group domain
(HMG). The octapeptide sequence (O) present in D-PAX2 is also shown. (B)
Binding of the Drosophila PAX6 and SOX2 homologues to the wild-type
monomeric DC5 sequence. Five nanograms of the tagged variants of the different
proteins were used in gel mobility shift assays. (C) Comparison of the binding
affinities of D-PAX2-PD, EY-PD and TOY-PD for the monomeric DC5 sequence.
(D,E,F) Cooperative binding of Drosophila PAX6/2 and SOX2 homologues
to the wild-type monomeric DC5 sequence. Combinations of the different tagged
variants were included in the binding reaction, and their ability to
cooperatively bind to the DC5 sequence was analysed by gel mobility shift
assays. In all the cases, the results were similar. The duplex complex SOX2
homologue-DC5 (red asterisks) migrated more slowly and became more intense
upon addition of increasing amounts of the PAX6/2 homologues, giving rise to
the triple complex SOX2 homologue-PAX6/2 homologue-DC5 (blue asterisks).
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