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A murine cardiac-specific homeodomain gene named csx (Komuro, I., and Izumo. S.(1993) Proc. Natl. Acad. Sci. U. S.
A. 90, 8145-8149) and nkx-2.5 (Lints, T. J.,
Parsons, L. M., Hartley, L., Lyons, I., and Harvey, R. P.(1993) Development 119, 419-431) was identified as a potential
vertebrate homologue of Drosophila tinman, a mesoderm
determination factor required for insect heart formation (Bodmer,
R.(1993) Development 118, 719-729). Bacterial expression
of the nkx-2.5 homeodomain allowed us to identify downstream
DNA targets from a library of randomly generated oligonucleotides. High
affinity nkx-2.5 DNA binding sites, 5`-TNNAGTG-3`, represented
novel binding sequences, whereas intermediate and weaker affinity
sites, 5`-C(A/T)TTAATTN-3`, contained the typical 5`-TAAT-3` core
required by most homeodomain factors for DNA binding. We also observed
that nkx-2.5 served as a modest transcription activator in
transfection assays done in 10T1/2 fibroblasts with multimerized
binding sites linked to a luciferase reporter gene. Functional
dissection of nkx-2.5 revealed a COOH-terminal inhibitory
domain composed mainly of clusters of alanines and prolines, which
appeared to mask a potent activation domain composed of hydrophobic and
highly charged amino acids.
Volume 270,
Number 26,
Issue of June 30, pp. 15628-15633, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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