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Nucleic Acids Research, 1992, Vol. 20, No. 17 4465-4472
© 1992

MOLECULAR BIOLOGY

Differential DNA binding properties of three human homeodomain proteins

Maria T. Corsetti1, Paola Briata1, Lorenza Sanseverino1,2, Antonio Daga1, Irma Airoldi1, Antonio Simeone3, Giulio Palmisano1, Cristiano Angelini1, Edoardo Boncinelli4 and Giorgio Corte1,2,*

1IST-Istituto Scientifico per la Ricerca sul Cancro 16132 Genoa 2Istituto di Chimica Biologica, Università di Genova 16132 Genoa 3IIGB, via Marconi 10, 80125 Naples 4Istituto Scientifico H.S.Raffaele 20132 Milan, Italy

*To whom correspondence should be addressed

Received June 12, 1992. Revised August 3, 1992. Accepted August 3, 1992.

The products of three human homeobox containing (HOX) genes, 2C, 3C and 4B, were produced in insect cells using the Baculovirus expression system and purified to near homogeneity. In this system we observed that the DNA binding forms of the three proteins are not glycosylated. HOX 3C and 4B are phosphorylated in insect cells, while HOX 2C is not. The three HOX proteins bind to a DNA sequence known to be a target site for Antennapedia protein with a very similar affinity (Kd = 1–2x10–9M). We then measured their binding properties to four human sequences present in the HOX 3D, 4C, 1C and 4B promoters. Two of these sequences have been reported to be binding sites for HOX proteins. HOX 2C, 3C and 4B behaved quite differently, showing low affinity for promoters of genes located upstream from their own gene in the HOX clusters and a higher affinity for regulatory sequences of their own gene and downstream HOX genes.


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