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Updated: Feb 14, 2026

Investigating Interactions Between Histone Modifying Enzymes and Transcription Factors in vivo by Fluorescence Resonance Energy Transfer
Published on: October 14, 2022
PRDM14, a putative histone methyl-transferase, interacts with and decreases the stability and activity of the HOXA1
Amandine Draime1, Laure Bridoux1, Magali Belpaire1
1Animal Molecular and Cellular Biology Group, Institut des Sciences de la Vie (ISV), Université catholique de Louvain, place Croix du Sud 5, 1348 Louvain-la-Neuve, Belgium.
Abstract:
Understanding how the activity of transcription factors like HOX proteins is regulated remains a widely open question. In a recent screen for proteins interacting with HOXA1, we identified a PRDM protein family member, PRDM14, which is known to be transiently co-expressed with HOXA1 in epiblast cells before their specification towards somatic versus germ cell fate. Here, we confirm PRDM14 is an interactor of HOXA1 and we identify the homeodomain of HOXA1 as well as the PR domain and Zinc fingers of PRDM14 to be required for the interaction. An 11-His repeat of HOXA1 previously highlighted to contribute to HOXA1-mediated protein-protein interactions is also involved. At a functional level, we provide evidence that HOXA1 displays an unexpectedly long half-life and demonstrate that PRDM14 can reduce the stability and affect the transcriptional activity of HOXA1.
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