# Novel Antennapedia and Ultrabithorax trimeric complexes with TBP and Exd regulate transcription

## TL;DR

This study identifies new protein interactions involving Antp and Ubx that form trimeric complexes with TBP and Exd, affecting transcriptional regulation.

## Contribution

The paper reports novel trimeric complexes of Antp, Ubx, TBP, and Exd, and a new interaction between Ubx and TBP.

## Key findings

- Antp interacts with Ubx via the homeodomain, requiring helixes 1 and 2 of AntpHD.
- Ubx interacts with TBP through the PolyQ domain of TBP.
- Two new trimeric complexes (Antp-Ubx-TBP-Exd) reduce Antp transcriptional activity.

## Abstract

Hox proteins interact with DNA and many other proteins, co-factors, transcriptional factors, chromatin remodeling components, non-coding RNAs and even the extracellular matrix that assembles the Hox complexes. The number of interacting partners continues to grow with diverse components and more transcriptional factors than initially thought. Hox complexes present many activities, but their molecular mechanisms to modulate their target genes remain unsolved.

In this paper we showed the protein-protein interaction of Antp with Ubx through the homeodomain using BiFC in Drosophila. Analysis of Antp-deletional mutants showed that AntpHD helixes 1 and 2 are required for the interaction with Ubx. Also, we found a novel interaction of Ubx with TBP, in which the PolyQ domain of TBP is required for the interaction. Moreover, we also detected the formation of two new trimeric complexes of Antp with Ubx, TBP and Exd using BiFC-FRET; these proteins, however, do not form a trimeric interaction with BIP2 or TFIIEβ. The novel trimeric complexes reduced Antp transcriptional activity, indicating that they could confer specificity for repression.

Our results increase the number of transcriptional factors in the Antp and Ubx interactomes that form two novel trimeric complexes with TBP and Exd. We also report a new Ubx interaction with TBP. These novel interactions provide important clues of the dynamics of Hox-interacting complexes involved in transcriptional regulation, contributing to better understand Hox function.

The online version contains supplementary material available at 10.1186/s41065-024-00327-x.