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Fig. 1. Comparison of protein and DNA sequence conservation of HyBra1 and
HyBra2. (A) Alignment of T-domains of HyBra1 and HyBra2 with
Brachyury proteins from mouse (M-T), Xenopus (X-bra), Amphioxus
(Am-bra-1), the sea urchin Hemicentrotus pulcherrimus (Hp-T), the
ascidian Halocynthia roretzi (As-T), Platynereis dumerilii
(Pd-bra) and Drosophila melanogaster (Dm-Trg). Amino acid identities
are black, partial identities (>60%) in grey. Amino acids marked by grey
dots under the sequence are involved in DNA-binding, grey bars indicate amino
acids involved in dimerisation
(Müller and Herrmann,
1997). Arrows indicate conserved intron sites in HyBra1
and mouse-T. (B) Alignment of the core repression module R1
(Kispert et al., 1994) within
the activation domain. HyBra2 and Drosophila Trg do not have
this motif. (C) Schematic structures of Xbra, HyBra1 and HyBra2 protein
illustrate the degree of amino acid identity in the T-box and the R1 domain
(blue box) in HyBra1 and HyBra2 compared with XBra.
(D) Comparison of exon-intron structure in Xbra, HyBra1 and
HyBra2. Filled boxes mark the ORF, white boxes the UTR. Red boxes
indicate conserved exon-intron sites, whereas black boxes indicate
non-conserved regions. Black numbers represent the length of introns.
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