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Determinants of T box protein specificity

Frank L. Conlon^*, Lynne Fairclough, Brenda M. J. Price, Elena S. Casey and J. C. Smith^,¶

Division of Developmental Biology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
^* Present address: Department of Genetics, Fordham Hall, UNC-Chapel Hill, Chapel Hill, NC 27599-3280, USA
Present address; Department of Molecular Biology, University of California, Berkeley, CA 94720, USA
Present address: Wellcome CRC Institute, Tennis Court Road, Cambridge CB2 1QR, UK

¶Author for correspondence (e-mail: jim{at}welc.cam.ac.uk)

We dedicate this paper to the memory of our friend and colleague Rosa Beddington

Accepted July 6, 2001

Members of the T box family of transcription factors play important roles in early development. Different members of the family exert different effects and here we show that much of the specificity of the Xenopus T box proteins Xbra, VegT and Eomesodermin resides in the DNA-binding domain, or T box. Binding site selection experiments show that the three proteins bind the same core sequence, but they select paired sites that differ in their orientation and spacing. Lysine 149 of Xbra is conserved in all Brachyury homologues, while the corresponding amino acid in VegT and Eomesodermin is asparagine. Mutation of this amino acid to lysine changes the inductive abilities of VegT and Eomesodermin to resemble that of Xbra.

Key words: T box genes, Brachyury, VegT, Eomesodermin, Xenopus

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