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Nucleic Acids Research, 1994, Vol. 22, No. 3 376-382
© 1994

MOLECULAR BIOLOGY

A proline-rich transcriptional activation domain in murine HOXD-4 (HOX-4.2)

Isabel Rambaldi1, Erzsebet Nagy Kovàcs1 and Mark S. Featherstone1,2,*

1McGill Cancer Centre. McGill University 3655 Drummond Street, Montréal, Québec H3G 1Y6, Canada 2Departments of Oncology and Medicine, McGill University 3655 Drummond Street, Montréal, Québec H3G 1Y6, Canada

*To whom correspondence should be addressed at: McGill Cancer Center, Room 714, 3655 Drummond Street, Montréal, Quebec H3G 1Y6, Canada

Received October 4, 1993. Accepted December 21, 1993.

The product of the murine Hoxd-4 (Hox-4.2) gene is a transcription factor that acts upon an autoregulatory element In Hoxd-4 upstream sequences (1). Using this activity as an assay In transient transfections of P19 embryonal carcinoma (EC) cells, we performed a mutatlonal analysis to map functional domains in the HOXD-4 protein. The importance of the homeodomaln was shown by a single amino acid change in this region that abolished activity. Deletion analysis revealed that many evolutlonarlly conserved regions outside of the homeodomain were dispensable for activation in our assay. Fusions to the GAL4 DNA-blndlng domain mapped a transcriptional activation function to the HOXD-4 proline-rich N-termlnus. The proline-rich transcription factor AP2 squelched activation by HOXD-4 and by GAL4/HOXD-4 N-termlnus fusion proteins. Together, these results suggest that HOXD-4 harbors a transcriptional activation domain of the proline-rlch type.


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