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Volume 272, Number 46, Issue of November 14, 1997 pp. 29151-29157
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Characterization and Retinoic Acid Responsiveness of the Murine Hoxd4 Transcription Unit

(Received for publication, May 16, 1997, and in revised form, July 18, 1997)

Adriana Folberg ^§ , Erszebet Nagy Kovács and Mark S. Featherstone ^§¶

From the  McGill Cancer Centre and the Departments of ^§ Medicine (Division of Experimental Medicine) and ^¶ Oncology, McGill University, 3655 Drummond St., Montréal, Québec H3G 1Y6, Canada

We have characterized the transcription unit of a murine Hox gene in the fourth paralogous group, Hoxd4. We have identified two Hoxd4 transcription start sites by S1 analysis. The upstream promoter (P2) is 5.2 kilobase pairs upstream from the coding region, while the downstream promoter (P1) is 1.1 kilobase pairs distant. Both promoters bear a cluster of start sites. Multiple transcripts were identified by Northern blot, originating from both promoters and multiple polyadenylation signals. Expression of P1 transcripts in the neural tube shows an anterior border at the rhombomere 6/7 boundary, corresponding to previous reports (Gaunt, S. J., Krumlauf, R., and Duboule, D. (1989) Development 107, 131-141; Morrison, A., Moroni, M. C., Ariza-McNaughton, L., Krumlauf, R., and Mavilio, F. (1996) Development 122, 1895-1907). A more posterior boundary in the central nervous system was observed for P2 transcripts. We observed strong expression up to somite 6 and weak expression in somite 5, correlating with the phenotype of Hoxd4 null mutant mice (Horan, G. S. B., Nagy Kovàcs, E., Behringer, R. R., and Featherstone, M. S. (1995) Dev. Biol. 169, 359-372). In response to retinoic acid, expression from P1 in the hindbrain was anteriorized after 4 or 24 h of treatment. P2 transcripts seemed to be less responsive and/or to have an indirect response to retinoic acid. The long 5-untranslated region found in all Hoxd4 transcripts suggests that translation does not occur by a classical ribosome scanning mechanism.

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