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Structure. 2015 Feb 3;23(2):270-9. doi: 10.1016/j.str.2014.12.011.

A flexible extension of the Drosophila ultrabithorax homeodomain defines a novel Hox/PBC interaction mode.

Author information

1
Centre National de la Recherche Scientifique, Aix-Marseille Université, CNRS UMR 7257, AFMB, 163 Avenue de Luminy, 13288 Marseille, France.
2
Centre National de la Recherche Scientifique, Aix-Marseille Université, CNRS UMR 7288, IBDM, Parc Scientifique de Luminy, Case 907, 13288 Marseille Cedex 09, France.
3
Centre National de la Recherche Scientifique, Aix-Marseille Université, CNRS UMR 7257, AFMB, 163 Avenue de Luminy, 13288 Marseille, France. Electronic address: miguel.ortiz-lombardia@univ-amu.fr.
4
Centre National de la Recherche Scientifique, Aix-Marseille Université, CNRS UMR 7288, IBDM, Parc Scientifique de Luminy, Case 907, 13288 Marseille Cedex 09, France. Electronic address: yacine.graba@univ-amu.fr.

Abstract

The patterning function of Hox proteins relies on assembling protein complexes with PBC proteins, which often involves a protein motif found in most Hox proteins, the so-called Hexapeptide (HX). Hox/PBC complexes likely gained functional diversity by acquiring additional modes of interaction. Here, we structurally characterize the first HX alternative interaction mode based on the paralogue-specific UbdA motif and further functionally validate structure-based predictions. The UbdA motif folds as a flexible extension of the homeodomain recognition helix and defines Hox/PBC contacts that occur, compared with those mediated by the HX motif, on the opposing side of the DNA double helix. This provides a new molecular facet to Hox/PBC complex assembly and suggests possible mechanisms for the diversification of Hox protein function.

PMID:
25651060
DOI:
10.1016/j.str.2014.12.011
[Indexed for MEDLINE]
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