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J Biol Chem, Vol. 273, Issue 21, 13273-13279, May 22, 1998
From the HOX proteins are dependent upon cofactors of the
PBX family for specificity of DNA binding. Two regions that have been
implicated in HOX/PBX cooperative interactions are the YPWM motif,
found N-terminal to the HOX homeodomain, and the GKFQ domain (also
known as the Hox cooperativity motif) immediately C-terminal to the PBX
homeodomain. Using derivatives of the E2A-PBX oncoprotein, we find that
the GKFQ domain is not essential for cooperative interaction with HOXA1
but contributes to the stability of the complex. By contrast, the YPWM
motif is strictly required for cooperative interactions in
vitro and in vivo, even with mutants of E2A-PBX
lacking the GKFQ domain. Using truncated PBX proteins, we show that the
YPWM motif contacts the PBX homeodomain. The presence of the GKFQ
domain increases monomer binding by the PBX homeodomain 5-fold, and the
stability of the HOXA1·E2A-PBX complex 2-fold. These data suggest
that the GKFQ domain acts mainly to increase DNA binding by PBX, rather
than providing a primary contact site for the YPWM motif of HOXA1. We
have identified 2 residues, Glu-301 and Tyr-305, required for GKFQ
function and suggest that this is dependent on
A Conserved C-terminal Domain in PBX Increases DNA Binding by
the PBX Homeodomain and Is Not a Primary Site of Contact for the
YPWM Motif of HOXA1
,,§, and§¶
McGill Cancer Centre, and Departments of
§ Medicine (Division of Experimental Medicine) and
¶ Oncology, McGill University,
Montréal, Québec H3G 1Y6, Canada
-helical
character.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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